2JIH
Crystal Structure of Human ADAMTS-1 catalytic Domain and Cysteine- Rich Domain (complex-form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 097 A1001 |
| Chain | Residue |
| A | ASP368 |
| A | SER432 |
| A | MET433 |
| A | LEU434 |
| A | ZN1553 |
| A | HOH2066 |
| A | HOH2122 |
| A | THR369 |
| A | LEU370 |
| A | GLY371 |
| A | HIS401 |
| A | GLU402 |
| A | HIS405 |
| A | HIS411 |
| A | ALA431 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 097 B1001 |
| Chain | Residue |
| B | ASP368 |
| B | THR369 |
| B | LEU370 |
| B | GLY371 |
| B | HIS401 |
| B | GLU402 |
| B | HIS405 |
| B | HIS411 |
| B | ALA431 |
| B | SER432 |
| B | MET433 |
| B | LEU434 |
| B | ZN1554 |
| B | HOH2087 |
| B | HOH2088 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1553 |
| Chain | Residue |
| A | HIS401 |
| A | HIS405 |
| A | HIS411 |
| A | 0971001 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1554 |
| Chain | Residue |
| B | HIS401 |
| B | HIS405 |
| B | HIS411 |
| B | 0971001 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD A1554 |
| Chain | Residue |
| A | GLU261 |
| A | ASP344 |
| A | ASP465 |
| A | HOH2038 |
| A | HOH2081 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A1555 |
| Chain | Residue |
| A | GLU315 |
| A | GLU320 |
| A | HOH2023 |
| A | HOH2026 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI A1556 |
| Chain | Residue |
| A | GLU494 |
| B | HIS313 |
| B | HOH2010 |
| B | HOH2022 |
| B | HOH2028 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A1557 |
| Chain | Residue |
| A | HIS280 |
| A | HOH2046 |
| B | ASP483 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD A1558 |
| Chain | Residue |
| A | GLU261 |
| A | ASP344 |
| A | ASP351 |
| A | CYS462 |
| A | ASP465 |
| A | HOH2080 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD B1555 |
| Chain | Residue |
| A | ASP483 |
| A | HOH2089 |
| B | HIS280 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI B1556 |
| Chain | Residue |
| A | HIS313 |
| B | GLU494 |
| B | ASP495 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD B1557 |
| Chain | Residue |
| B | GLU261 |
| B | ASP344 |
| B | ASP465 |
| B | HOH2026 |
| B | HOH2063 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B1558 |
| Chain | Residue |
| B | GLU261 |
| B | ASP344 |
| B | ASP351 |
| B | CYS462 |
| B | ASP465 |
| B | HOH2061 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI B1559 |
| Chain | Residue |
| A | HIS313 |
| A | HOH2009 |
| B | GLU494 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI A1559 |
| Chain | Residue |
| A | GLU320 |
| A | HOH2024 |
| A | HOH2025 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A1560 |
| Chain | Residue |
| A | HIS339 |
| A | HOH2035 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI A1561 |
| Chain | Residue |
| A | HIS428 |
| A | HOH2064 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI A1562 |
| Chain | Residue |
| A | GLU494 |
| A | ASP495 |
| B | HIS313 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI A1563 |
| Chain | Residue |
| A | HIS498 |
| A | HOH2100 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NI A1564 |
| Chain | Residue |
| A | HIS525 |
| A | HOH2073 |
| A | HOH2104 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B1560 |
| Chain | Residue |
| B | HIS439 |
| B | ASP530 |
| B | ASN542 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI B1561 |
| Chain | Residue |
| B | HIS428 |
| B | HOH2051 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B1562 |
| Chain | Residue |
| B | HIS459 |
| site_id | CC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NI B1563 |
| Chain | Residue |
| B | HIS498 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A1565 |
| Chain | Residue |
| A | ASP360 |
| A | LEU361 |
| A | CYS367 |
| A | THR369 |
| A | GLU389 |
| A | NA1566 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A1566 |
| Chain | Residue |
| A | ASP360 |
| A | CYS367 |
| A | NA1565 |
| A | HOH2050 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A1567 |
| Chain | Residue |
| A | PRO410 |
| A | ASP412 |
| A | MET430 |
| A | SER447 |
| site_id | DC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NA B1564 |
| Chain | Residue |
| B | ASP360 |
| B | LEU361 |
| B | CYS367 |
| B | ASP368 |
| B | THR369 |
| B | GLU389 |
| B | NA1565 |
| B | HOH2039 |
| site_id | DC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B1565 |
| Chain | Residue |
| B | ASP360 |
| B | CYS367 |
| B | NA1564 |
| B | HOH2039 |
| site_id | DC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NI A1568 |
| Chain | Residue |
| A | HIS439 |
| A | HOH2069 |
| site_id | DC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A1569 |
| Chain | Residue |
| A | VAL518 |
| A | LEU519 |
| B | HIS525 |
| site_id | DC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B1566 |
| Chain | Residue |
| B | HIS339 |
| site_id | DC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B1567 |
| Chain | Residue |
| B | HIS439 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGeDSKHCPD |
| Chain | Residue | Details |
| A | PHE492-ASP501 |
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TTAHELGHVF |
| Chain | Residue | Details |
| A | THR398-PHE407 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17897672","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17897672","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
