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8ZJF

Cryo-EM structure of human integrin alpha-E beta-7

Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CsCapGrlGRlC
ChainResidueDetails
BCYS500-CYS511
BCYS548-CYS559
BCYS585-CYS596
BCYS624-CYS635

site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CdQCPgCKtPCE
ChainResidueDetails
BCYS635-GLU646

site_idPS00242
Number of Residues8
DetailsINTEGRIN_ALPHA Integrins alpha chain signature. FKcGFFkR
ChainResidueDetails
APHE1147-ARG1154

site_idPS00243
Number of Residues14
DetailsINTEGRIN_BETA Integrins beta chain cysteine-rich domain signature. CsGk..GhCqCgrCsC
ChainResidueDetails
BCYS537-CYS550
BCYS574-CYS587
BCYS613-CYS626

site_idPS01186
Number of Residues15
DetailsEGF_2 EGF-like domain signature 2. CqCldGYygalcdq.C
ChainResidueDetails
BCYS624-CYS638

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1105
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
APHE19-SER1124

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ALEU1125-PHE1147

site_idSWS_FT_FI3
Number of Residues31
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ALYS1148-ASN1179

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P08648
ChainResidueDetails
AASP522
ASER656
AASP658
AASP662
AASP524
AASP526
AASP530
AASP586
ASER588
AASP590
AASP594
AASP654

site_idSWS_FT_FI5
Number of Residues11
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN49
AASN1065
AASN1096
AASN271
AASN321
AASN444
AASN726
AASN782
AASN857
AASN934
AASN954

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P
ChainResidueDetails
BASP167

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
ChainResidueDetails
BASP198
BASN254
BASP256
BPRO258

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
ChainResidueDetails
BGLU259

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and liganded-open conformation => ECO:0000250|UniProtKB:P05107
ChainResidueDetails
BASP289

site_idSWS_FT_FI10
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
ChainResidueDetails
BGLU373

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by Tyr-kinases => ECO:0000250
ChainResidueDetails
BTYR778

site_idSWS_FT_FI12
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN68
BASN477
BASN531
BASN590
BASN665
BASN674

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V
ChainResidueDetails
BASN279

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V
ChainResidueDetails
BASN434

221716

PDB entries from 2024-06-26

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