4ZW6
X-ray crystal structure of PfA-M1 in complex with hydroxamic acid-based inhibitor 9q
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue 4SY A 1101 |
Chain | Residue |
A | THR305 |
A | HIS500 |
A | GLU519 |
A | TYR575 |
A | TYR580 |
A | MET1034 |
A | ZN1102 |
A | GOL1107 |
A | HOH1243 |
A | HOH1721 |
A | GLU319 |
A | VAL459 |
A | GLY460 |
A | ALA461 |
A | GLU463 |
A | ARG489 |
A | HIS496 |
A | GLU497 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1102 |
Chain | Residue |
A | HIS496 |
A | HIS500 |
A | GLU519 |
A | 4SY1101 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue MG A 1103 |
Chain | Residue |
A | HOH1269 |
A | HOH1407 |
A | HOH1787 |
A | HOH2012 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue MG A 1104 |
Chain | Residue |
A | GLU679 |
A | HOH1493 |
A | HOH1798 |
A | HOH1941 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG A 1105 |
Chain | Residue |
A | HOH1327 |
A | HOH1491 |
A | HOH1607 |
A | HOH1945 |
A | HOH2007 |
A | HOH2015 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue GOL A 1106 |
Chain | Residue |
A | VAL459 |
A | GLY460 |
A | ASN471 |
A | ASN473 |
A | SER474 |
A | ARG489 |
A | ASN994 |
A | ARG997 |
A | HOH1202 |
A | HOH1252 |
A | HOH1517 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GOL A 1107 |
Chain | Residue |
A | TYR575 |
A | TYR580 |
A | 4SY1101 |
A | HOH1231 |
A | HOH1253 |
A | HOH1481 |
A | HOH1777 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GOL A 1108 |
Chain | Residue |
A | TYR853 |
A | SER903 |
A | LEU904 |
A | DMS1111 |
A | HOH1669 |
A | HOH1769 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue DMS A 1109 |
Chain | Residue |
A | ASN573 |
A | HOH1253 |
A | HOH1295 |
A | HOH1360 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue DMS A 1110 |
Chain | Residue |
A | ASP758 |
A | SER759 |
A | ALA761 |
A | ARG764 |
A | HOH1979 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue DMS A 1111 |
Chain | Residue |
A | TYR853 |
A | THR900 |
A | SER903 |
A | LEU904 |
A | GOL1108 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue DMS A 1112 |
Chain | Residue |
A | SER822 |
A | TYR823 |
A | THR900 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue PO4 A 1113 |
Chain | Residue |
A | VAL245 |
A | ASP247 |
A | PHE275 |
A | HOH1405 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue PO4 A 1114 |
Chain | Residue |
A | SER396 |
A | ALA397 |
A | THR398 |
A | GLU409 |
A | TYR411 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVGHEYFHQY |
Chain | Residue | Details |
A | VAL493-TYR502 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P15144 |
Chain | Residue | Details |
A | GLU497 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:19196988, ECO:0000305|PubMed:21366301, ECO:0007744|PDB:3EBH, ECO:0007744|PDB:3EBI, ECO:0007744|PDB:3Q43 |
Chain | Residue | Details |
A | GLU319 | |
A | GLY460 | |
A | GLU463 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:19196988, ECO:0000305|PubMed:21366301, ECO:0007744|PDB:3EBH, ECO:0007744|PDB:3Q43 |
Chain | Residue | Details |
A | ALA461 |
Chain | Residue | Details |
A | HIS496 | |
A | HIS500 | |
A | GLU519 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for substrate specificity => ECO:0000269|PubMed:23897806 |
Chain | Residue | Details |
A | VAL459 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P15144 |
Chain | Residue | Details |
A | TYR580 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Cleavage => ECO:0000305|PubMed:21659511 |
Chain | Residue | Details |
A | GLN795 |