3JTS

Mamu-A1*002:01 binding "GSENLKSLY" at 2.80Å resolution

Data provenance

Structure downloaded from PDB Europe using the Coordinate Server. Aligned to residues 1-180 of 1HHK2 using the CEALIGN3 function of PyMol4. Chain assigment using a Levenshtein distance5 method using data from the PDBe REST API6. Organism data from PDBe REST API. Data for both of these operations from the Molecules endpoint. Structure visualised with 3DMol7.

Complex type

Class i with peptide

1. Beta 2 microglobulin

['B', 'E', 'H']

2. Class I alpha
Mamu-A1*002:01

['A', 'D', 'G']

3. Peptide
GSENLKSLY

['C', 'F', 'I']

Species

Macaca mulatta (rhesus monkey)

Locus / Allele group

MAMU-A1 / Mamu-A1*002

Publication

Structure of Mamu A*2

Dai, L.

Structure deposition and release

Deposited: 2009-09-14

Released: 2010-09-15

Revised: 2011-07-13

Data provenance

Publication data retrieved from PDBe REST API8 and PMCe REST API9

Other structures from this publication

Peptide details

Length: Nonamer (9 amino acids)

Sequence: GSENLKSLY

Interactive view

Cutaway side view (static)

Surface top view (static - coloured by atom property)

Cutaway top view (static)

Data provenance

MHC:peptide complexes are visualised using PyMol. The peptide is superimposed on a consistent cutaway slice of the MHC binding cleft (displayed as a grey mesh) which best indicates the binding pockets for the P1/P5/PC positions (side view - pockets A, E, F) and for the P2/P3/PC-2 positions (top view - pockets B, C, D). In some cases peptides will use a different pocket for a specific peptide position (atypical anchoring). On some structures the peptide may appear to sterically clash with a pocket. This is an artefact of picking a standardised slice of the cleft and overlaying the peptide.

Peptide neighbours

P1 GLY

MET5

TYR59

TYR7

GLU63

TRP167

PHE33

TYR171

TYR159

P2 SER

TYR99

GLU63

MET67

TYR159

GLU163

TYR9

ARG62

ASN66

MET45

TYR7

P3 GLU

TYR159

TYR99

TYR9

ASN66

HIS114

HIS156

GLN155

P4 ASN

ASN66

ALA69

P5 LEU

HIS114

GLU152

HIS156

GLU70

TYR99

ARG97

TYR9

P6 LYS

GLN155

GLU152

P7 SER

ASN73

ALA150

TRP147

GLU152

ASN77

P8 LEU

VAL76

LYS146

THR143

ASN73

ASN80

TRP147

ASN77

P9 TYR

TYR84

ARG97

TYR123

ILE95

LYS146

TRP147

THR143

LEU81

ASN142

GLN96

ASN77

ASN80

SER116

ILE124

Colour key

Aromatic Hydrophobic Acidic Basic Neutral/polar

Data provenance

Neighbours are calculated by finding residues with atoms within 5Å of each other using BioPython Neighboursearch module. The list of neighbours is then sorted and filtered to inlcude only neighbours where between the peptide and the MHC Class I alpha chain.

Colours selected to match the YRB scheme. [https://www.frontiersin.org/articles/10.3389/fmolb.2015.00056/full]

Binding cleft pockets

Peptide sidechain binding pockets (static)

Peptide terminii and backbone binding residues (static)

A Pocket

TYR159

GLU163

TRP167

TYR171

MET5

TYR59

GLU63

ASN66

TYR7

B Pocket

ALA24

VAL34

MET45

GLU63

ASN66

MET67

TYR7

GLU70

TYR9

TYR99

C Pocket

GLU70

ASN73

ALA74

TYR9

ARG97

D Pocket

HIS114

GLN155

HIS156

TYR159

LEU160

TYR99

E Pocket

HIS114

TRP147

GLU152

HIS156

ARG97

F Pocket

SER116

TYR123

THR143

LYS146

TRP147

ASN77

ASN80

LEU81

TYR84

ILE95

Colour key

Binds N-terminus Binds P1 backbone Binds P2 backbone Binds PC-1 backbone Binds C-terminus

Data provenance

N-/C-terminus and peptide backbone binding residues are assigned according to previously published information and pockets are assigned according to an adaptation of a previously published set of residues. All numbering is currently that of the 'canonical' structures of human and mouse MHC Class I molecules.

Chain sequences

1. Beta 2 microglobulin Beta 2 microglobulin	10 20 30 40 50 60 MSRSVALAVLALLSLSGLEAIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLL 70 80 90 100 110 KNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

2. Class I alpha Mamu-A1002:01 IPD-MHC* [ipd-mhc:NHP10428]	10 20 30 40 50 60 GSHSMRYFYTSMSRPGRWEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWVEQEGPEYW 70 80 90 100 110 120 DRETRNMKAETQNAPVNLRNLRGYYNQSEAGSHTIQRMYGCDLGPDGRLLRGYHQSAYDG 130 140 150 160 170 180 KDYIALNEDLRSWTAADMAAQNTQRKWEAAGEAEQHRTYLEGECLEWLRRYLENGKETLQ 190 200 210 220 230 240 RADPPKTHVTHHPVSDQEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT 250 260 270 FQKWAAVVVPSGKEQRYTCHVQHEGLREPLTLRWEP

3. Peptide	GSENLKSLY

Data provenance

Sequences are retrieved via the Uniprot method of the RSCB REST API. Sequences are then compared to those derived from the PDB file and matched against sequences retrieved from the IPD-IMGT/HLA database for human sequences, or the IPD-MHC database for other species. Mouse sequences are matched against FASTA files from Uniprot. Sequences for the mature extracellular protein (signal petide and cytoplasmic tail removed) are compared to identical length sequences from the datasources mentioned before using either exact matching or Levenshtein distance based matching.

Downloadable data

Data can be downloaded to your local machine from the links below.

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e.g. load http://www.histo.fyi/structures/downloads/1hhk_1_peptide.cif

or in the case of JSON formatted files to retrieve it and use it as part of notebooks such as Jupyter or GoogleColab.

Please take note of the data license. Using data from this site assumes that you have read and will comply with the license.

Complete structures

Aligned structures [cif]

Components

MHC Class I alpha chain [cif]

MHC Class I antigen binding domain (alpha1/alpha2) [cif]

Peptide only [cif]

Derived data

Data for this page [json]

https://api.histo.fyi/v1/structures/3jts

Data license

The data above is made available under a Creative Commons CC-BY 4.0 license. This means you can copy, remix, transform, build upon and redistribute the material, but you must give appropriate credit, provide a link to the license, and indicate if changes were made.

If you use any data downloaded from this site in a publication, please cite 'https://www.histo.fyi/'. A preprint is in preparation.

Footnotes

Protein Data Bank Europe - Coordinate Server
1HHK - HLA-A*02:01 binding LLFGYPVYV at 2.5Å resolution - PDB entry for 1HHK
Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. - PyMol CEALIGN Method - Publication
PyMol - PyMol.org/pymol
Levenshtein distance - Wikipedia entry
Protein Data Bank Europe REST API - Molecules endpoint
3Dmol.js: molecular visualization with WebGL - 3DMol.js - Publication
Protein Data Bank Europe REST API - Publication endpoint
PubMed Central Europe REST API - Articles endpoint

This work is licensed under a Creative Commons Attribution 4.0 International License.