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

5NEU

Localised Reconstruction of Integrin alpha V beta 6 bound to Foot and Mouth Disease Virus O1 Manisa - Pose B.

Functional Information from GO Data
ChainGOidnamespacecontents
10005198molecular_functionstructural molecule activity
10019028cellular_componentviral capsid
20005198molecular_functionstructural molecule activity
30005198molecular_functionstructural molecule activity
40019030cellular_componenticosahedral viral capsid
A0007155biological_processcell adhesion
A0008305cellular_componentintegrin complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG 1 2001
ChainResidue
1ASP147
BASP102
BSER104
BGLU202
BALA234

site_idAC2
Number of Residues5
Detailsbinding site for residue CA B 601
ChainResidue
BGLU202
BGLU141
BASN197
BASP199
BPRO201

site_idAC3
Number of Residues4
Detailsbinding site for residue CA B 602
ChainResidue
BASP109
BASP110
BLYS317
BASP318

Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CaChpGhmGPrC
ChainResidueDetails
BCYS527-CYS538

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
BASP102
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
BSER104
BGLU202

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: in MIDAS binding site => ECO:0000250|UniProtKB:P05106
ChainResidueDetails
BSER106
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
BASP109
BASP110

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: in LIMBS binding site => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM9
ChainResidueDetails
BGLU141
BASN197
BASP199
BPRO201

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and liganded-open conformation => ECO:0000250|UniProtKB:P05106
ChainResidueDetails
BASP233

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
BLYS317

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
BASN26
BASN59
BASN436

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
BASN222

site_idSWS_FT_FI10
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN445
BASN511
BASN519

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon