4BTY
Crystal structure of human vascular adhesion protein-1 in complex with pyridazinone inhibitors
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005769 | cellular_component | early endosome |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005902 | cellular_component | microvillus |
| A | 0006954 | biological_process | inflammatory response |
| A | 0007155 | biological_process | cell adhesion |
| A | 0008131 | molecular_function | primary amine oxidase activity |
| A | 0009308 | biological_process | amine metabolic process |
| A | 0009986 | cellular_component | cell surface |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0048038 | molecular_function | quinone binding |
| A | 0052595 | molecular_function | aliphatic amine oxidase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005769 | cellular_component | early endosome |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005902 | cellular_component | microvillus |
| B | 0006954 | biological_process | inflammatory response |
| B | 0007155 | biological_process | cell adhesion |
| B | 0008131 | molecular_function | primary amine oxidase activity |
| B | 0009308 | biological_process | amine metabolic process |
| B | 0009986 | cellular_component | cell surface |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0048038 | molecular_function | quinone binding |
| B | 0052595 | molecular_function | aliphatic amine oxidase activity |
Functional Information from PROSITE/UniProt
| site_id | PS01164 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVrsmsTllNYDY |
| Chain | Residue | Details |
| A | LEU460-TYR473 |
| site_id | PS01165 |
| Number of Residues | 14 |
| Details | COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TaGflHIphaEDiP |
| Chain | Residue | Details |
| A | THR679-PRO692 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1472 |
| Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:9653080 |
| Chain | Residue | Details |
| B | GLY27-ASN763 | |
| A | GLY27-ASN763 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P19801 |
| Chain | Residue | Details |
| A | ASP386 | |
| B | ASP386 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:16046623, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1 |
| Chain | Residue | Details |
| A | TPQ471 | |
| B | TPQ471 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 26 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY |
| Chain | Residue | Details |
| A | ASP529 | |
| A | LEU530 | |
| A | ASP531 | |
| A | GLU572 | |
| A | GLU641 | |
| A | PHE663 | |
| A | ASN665 | |
| A | GLU667 | |
| A | ASP673 | |
| A | LEU674 | |
| A | HIS684 | |
| B | HIS520 | |
| B | HIS522 | |
| B | ASP529 | |
| B | LEU530 | |
| B | ASP531 | |
| B | GLU572 | |
| B | GLU641 | |
| B | PHE663 | |
| B | ASN665 | |
| B | GLU667 | |
| B | ASP673 | |
| B | LEU674 | |
| B | HIS684 | |
| A | HIS520 | |
| A | HIS522 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:16046623, ECO:0007744|PDB:1PU4 |
| Chain | Residue | Details |
| A | TPQ471 | |
| B | TPQ471 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GalNAc...) serine => ECO:0000305|PubMed:16046623 |
| Chain | Residue | Details |
| A | SER43 | |
| B | SER43 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1 |
| Chain | Residue | Details |
| A | ASN137 | |
| B | ASN137 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000305|PubMed:16046623 |
| Chain | Residue | Details |
| A | THR212 | |
| B | THR212 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:1PU4, ECO:0007744|PDB:1US1, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY |
| Chain | Residue | Details |
| A | ASN232 | |
| B | ASN232 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTY |
| Chain | Residue | Details |
| A | ASN294 | |
| B | ASN294 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY |
| Chain | Residue | Details |
| B | ASN592 | |
| A | ASN592 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX |
| Chain | Residue | Details |
| B | ASN618 | |
| A | ASN618 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16046623, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24304424, ECO:0007744|PDB:4BTW, ECO:0007744|PDB:4BTX, ECO:0007744|PDB:4BTY |
| Chain | Residue | Details |
| B | ASN666 | |
| A | ASN666 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GlcNAc) threonine => ECO:0000305|PubMed:16046623 |
| Chain | Residue | Details |
| A | THR679 | |
| B | THR679 |
