Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5NEM

Localised reconstruction of alpha v beta 6 bound to Foot and Mouth Disease Virus O PanAsia - Pose A.

Functional Information from GO Data
ChainGOidnamespacecontents
10005198molecular_functionstructural molecule activity
10019028cellular_componentviral capsid
10019062biological_processvirion attachment to host cell
10046718biological_processsymbiont entry into host cell
20005198molecular_functionstructural molecule activity
30005198molecular_functionstructural molecule activity
40019030cellular_componenticosahedral viral capsid
A0007155biological_processcell adhesion
A0008305cellular_componentintegrin complex
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CaChpGhmGPrC
ChainResidueDetails
BCYS459-CYS470

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: in MIDAS binding site => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8
ChainResidueDetails
BASP120
APHE294
AASP351
AASP353
APHE355
AASP357
AALA359
AASP415
AASN417
ATYR419
AASP421
AASP234
AILE423
AILE236
AASP238
AVAL240
AASN286
AASP288
ATYR290
AASP292

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: in MIDAS binding site => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8, ECO:0007744|PDB:4UM9
ChainResidueDetails
BSER122
BGLU220

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: in MIDAS binding site => ECO:0000250|UniProtKB:P05106
ChainResidueDetails
BSER124
ATHR268
ATHR460
ASER528

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: in ADMIDAS binding site => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8, ECO:0007744|PDB:4UM9
ChainResidueDetails
BASP127
BASP128

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: in LIMBS binding site => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM9
ChainResidueDetails
BGLU159
BASN215
BASP217
BPRO219

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and liganded-open conformation => ECO:0000250|UniProtKB:P05106
ChainResidueDetails
BASP251

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8
ChainResidueDetails
BLYS335

site_idSWS_FT_FI8
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8, ECO:0007744|PDB:4UM9
ChainResidueDetails
BASN28
BASN77
BASN367

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:25383667, ECO:0000269|PubMed:28117447, ECO:0007744|PDB:4UM8, ECO:0007744|PDB:4UM9
ChainResidueDetails
BASN240

site_idSWS_FT_FI10
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN376
BASN443
BASN451

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon