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

8GCE

The Extracellular Domain of Integrin AlphaIIbBeta3 in Intermediate State

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0008305cellular_componentintegrin complex
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CrCgpGwlGSqC
ChainResidueDetails
BCYS460-CYS471
BCYS547-CYS558

site_idPS00242
Number of Residues8
DetailsINTEGRIN_ALPHA Integrins alpha chain signature. WKvGFFkR
ChainResidueDetails
ATRP988-ARG995

site_idPS00243
Number of Residues14
DetailsINTEGRIN_BETA Integrins beta chain cysteine-rich domain signature. CsQr..GeClCgqCvC
ChainResidueDetails
BCYS495-CYS508
BCYS536-CYS549
BCYS575-CYS588

site_idPS01186
Number of Residues14
DetailsEGF_2 EGF-like domain signature 2. CrCgpGWlgsqce..C
ChainResidueDetails
BCYS460-CYS473

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues691
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BGLY1-ASP692

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BILE693-TRP715

site_idSWS_FT_FI3
Number of Residues46
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BLYS716-THR762

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
ChainResidueDetails
BSER121
AASP305
AASP365
AASP367
AASP369
ATYR371
AASP373
AASP426
AASP428
AASN430
ATYR432
BGLU220
AASP434
AASP247
ATHR250
AGLU252
AASP297
AASN299
AASP301
AARG303

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: in MIDAS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCU
ChainResidueDetails
BSER123

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: in ADMIDAS binding site => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU, ECO:0007744|PDB:3IJE
ChainResidueDetails
BASP126
BASP127

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: in LIMBS binding site => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3FCU
ChainResidueDetails
BASP158
BASN215
BASP217
BPRO219

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: in LIMBS binding site => ECO:0007744|PDB:4G1M
ChainResidueDetails
BASP251

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:3FCS, ECO:0007744|PDB:3IJE
ChainResidueDetails
BMET335

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O54890
ChainResidueDetails
BTHR741

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19141530, ECO:0007744|PubMed:18088087
ChainResidueDetails
BTYR747

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 and PKB/AKT1; in vitro => ECO:0000269|PubMed:10896934
ChainResidueDetails
BTHR753

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8631894
ChainResidueDetails
BTYR759

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE
ChainResidueDetails
BASN99

site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:15378069, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:1TYE, ECO:0007744|PDB:3IJE
ChainResidueDetails
BASN320
BASN371

site_idSWS_FT_FI16
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:3IJE
ChainResidueDetails
BASN452

site_idSWS_FT_FI17
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:19111664, ECO:0000269|PubMed:19704023, ECO:0007744|PDB:1JV2, ECO:0007744|PDB:3IJE
ChainResidueDetails
BASN559

site_idSWS_FT_FI18
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11546839, ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1JV2
ChainResidueDetails
BASN654

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon