8ZJF
Cryo-EM structure of human integrin alpha-E beta-7
Functional Information from PROSITE/UniProt
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CsCapGrlGRlC |
Chain | Residue | Details |
B | CYS500-CYS511 | |
B | CYS548-CYS559 | |
B | CYS585-CYS596 | |
B | CYS624-CYS635 |
site_id | PS00198 |
Number of Residues | 12 |
Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CdQCPgCKtPCE |
Chain | Residue | Details |
B | CYS635-GLU646 |
site_id | PS00242 |
Number of Residues | 8 |
Details | INTEGRIN_ALPHA Integrins alpha chain signature. FKcGFFkR |
Chain | Residue | Details |
A | PHE1147-ARG1154 |
site_id | PS00243 |
Number of Residues | 14 |
Details | INTEGRIN_BETA Integrins beta chain cysteine-rich domain signature. CsGk..GhCqCgrCsC |
Chain | Residue | Details |
B | CYS537-CYS550 | |
B | CYS574-CYS587 | |
B | CYS613-CYS626 |
site_id | PS01186 |
Number of Residues | 15 |
Details | EGF_2 EGF-like domain signature 2. CqCldGYygalcdq.C |
Chain | Residue | Details |
B | CYS624-CYS638 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1105 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | PHE19-SER1124 |
site_id | SWS_FT_FI2 |
Number of Residues | 22 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | LEU1125-PHE1147 |
site_id | SWS_FT_FI3 |
Number of Residues | 31 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | LYS1148-ASN1179 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P08648 |
Chain | Residue | Details |
A | ASP522 | |
A | SER656 | |
A | ASP658 | |
A | ASP662 | |
A | ASP524 | |
A | ASP526 | |
A | ASP530 | |
A | ASP586 | |
A | SER588 | |
A | ASP590 | |
A | ASP594 | |
A | ASP654 |
site_id | SWS_FT_FI5 |
Number of Residues | 11 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN49 | |
A | ASN1065 | |
A | ASN1096 | |
A | ASN271 | |
A | ASN321 | |
A | ASN444 | |
A | ASN726 | |
A | ASN782 | |
A | ASN857 | |
A | ASN934 | |
A | ASN954 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: in ADMIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P |
Chain | Residue | Details |
B | ASP167 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: in LIMBS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V |
Chain | Residue | Details |
B | ASP198 | |
B | ASN254 | |
B | ASP256 | |
B | PRO258 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | BINDING: in MIDAS binding site => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V |
Chain | Residue | Details |
B | GLU259 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | BINDING: in ADMIDAS binding site and liganded-open conformation => ECO:0000250|UniProtKB:P05107 |
Chain | Residue | Details |
B | ASP289 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | BINDING: in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V |
Chain | Residue | Details |
B | GLU373 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by Tyr-kinases => ECO:0000250 |
Chain | Residue | Details |
B | TYR778 |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN68 | |
B | ASN477 | |
B | ASN531 | |
B | ASN590 | |
B | ASN665 | |
B | ASN674 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4P, ECO:0007744|PDB:3V4V |
Chain | Residue | Details |
B | ASN279 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22232704, ECO:0007744|PDB:3V4V |
Chain | Residue | Details |
B | ASN434 |