3HYG
Crystal Structure of the Catalytic Domain of ADAMTS-5 in Complex with an Amino-2-indanol compound
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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 901 |
Chain | Residue |
A | HIS410 |
A | HIS414 |
A | HIS420 |
A | 099801 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 902 |
Chain | Residue |
A | HOH5001 |
A | GLU270 |
A | ASP353 |
A | ASP360 |
A | CYS471 |
A | ASP474 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 903 |
Chain | Residue |
A | GLU270 |
A | ASP353 |
A | ASP474 |
A | HOH5014 |
A | HOH5018 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 904 |
Chain | Residue |
A | ASP369 |
A | LEU370 |
A | CYS376 |
A | THR378 |
A | GLU398 |
A | HOH5030 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 099 A 801 |
Chain | Residue |
A | ASP377 |
A | THR378 |
A | LEU379 |
A | GLY380 |
A | THR407 |
A | HIS410 |
A | GLU411 |
A | HIS414 |
A | HIS420 |
A | LEU438 |
A | SER440 |
A | SER441 |
A | ILE442 |
A | LEU443 |
A | ZN901 |
A | HOH5023 |
A | HOH5025 |
A | HOH5131 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 901 |
Chain | Residue |
B | HIS410 |
B | HIS414 |
B | HIS420 |
B | 099801 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 902 |
Chain | Residue |
B | GLU270 |
B | ASP353 |
B | ASP360 |
B | CYS471 |
B | ASP474 |
B | HOH6010 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 903 |
Chain | Residue |
B | GLU270 |
B | ASP353 |
B | ASP474 |
B | HOH6037 |
B | HOH6119 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 904 |
Chain | Residue |
B | ASP369 |
B | LEU370 |
B | CYS376 |
B | THR378 |
B | GLU398 |
B | HOH6009 |
site_id | BC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 099 B 801 |
Chain | Residue |
B | ASP377 |
B | THR378 |
B | LEU379 |
B | GLY380 |
B | THR407 |
B | HIS410 |
B | GLU411 |
B | HIS414 |
B | HIS420 |
B | LEU438 |
B | SER440 |
B | SER441 |
B | LEU443 |
B | ZN901 |
B | HOH6023 |
B | HOH6039 |
B | HOH6085 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVAHEIGHLL |
Chain | Residue | Details |
A | THR407-LEU416 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 418 |
Details | Domain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
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":"18042673","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"18042673","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |