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8XER

Cryo-EM structure of integrin ITGAV, ITGB3 and Cilengitide TFA complex, conformation 1

This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CrCgpGwlGSqC
ChainResidueDetails
BCYS486-CYS497
BCYS573-CYS584

site_idPS00242
Number of Residues8
DetailsINTEGRIN_ALPHA Integrins alpha chain signature. YRmGFFkR
ChainResidueDetails
ATYR1016-ARG1023

site_idPS00243
Number of Residues14
DetailsI_EGF_1 Integrins beta chain EGF (I-EGF) domain signature. CsQr..GeClCgqCvC
ChainResidueDetails
BCYS521-CYS534
BCYS562-CYS575
BCYS601-CYS614

site_idPS01186
Number of Residues14
DetailsEGF_2 EGF-like domain signature 2. CrCgpGWlgsqce..C
ChainResidueDetails
BCYS486-CYS499

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues691
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BGLY27-ASP718

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BILE719-TRP741

site_idSWS_FT_FI3
Number of Residues46
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BLYS742-THR788

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
BSER147
AASP322
AASP379
AASP381
AASP383
APHE385
AASP387
AASP443
AASP445
AASN447
ATYR449
BGLU246
AASP451
AASP264
AILE266
AASP268
AASP314
AASN316
AASP318
ATYR320

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
BSER149

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
BASP152
BASP153
AASN488
AASN554

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
BASP184
BASN241
BASP243
BPRO245

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: in LIMBS binding site => ECO:0007744|PDB:4G1M
ChainResidueDetails
BASP277

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
BMET361
AASN973
AASN980

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O54890
ChainResidueDetails
BTHR767
AASN945

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19141530, ECO:0007744|PubMed:18088087
ChainResidueDetails
BTYR773

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 and PKB/AKT1; in vitro => ECO:0000269|PubMed:10896934
ChainResidueDetails
BTHR779

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8631894
ChainResidueDetails
BTYR785

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
BASN125

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
BASN346
BASN397

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
BASN478

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
BASN585

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
BASN680

229183

PDB entries from 2024-12-18

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