6EED
X-ray crystal structure of Pf-M1 in complex with inhibitor (6p) and catalytic zinc ion
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1101 |
Chain | Residue |
A | HIS496 |
A | HIS500 |
A | GLU519 |
A | J6A1102 |
site_id | AC2 |
Number of Residues | 24 |
Details | binding site for residue J6A A 1102 |
Chain | Residue |
A | VAL459 |
A | GLY460 |
A | ALA461 |
A | GLU463 |
A | HIS496 |
A | GLU497 |
A | HIS500 |
A | GLU519 |
A | GLU572 |
A | TYR575 |
A | THR576 |
A | TYR580 |
A | MET1034 |
A | ZN1101 |
A | PO41115 |
A | HOH1277 |
A | HOH1540 |
A | HOH1694 |
A | HOH1839 |
A | THR305 |
A | GLN317 |
A | GLU319 |
A | ALA320 |
A | ASN458 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 1103 |
Chain | Residue |
A | GLY250 |
A | HOH1818 |
A | HOH1870 |
A | HOH1954 |
A | HOH1964 |
A | HOH2037 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue MG A 1104 |
Chain | Residue |
A | GLU957 |
A | HOH1377 |
A | HOH1396 |
A | HOH1787 |
A | HOH2304 |
A | HOH2504 |
A | HOH2532 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG A 1105 |
Chain | Residue |
A | HOH1424 |
A | HOH1689 |
A | HOH1937 |
A | HOH2285 |
A | HOH2447 |
A | HOH2620 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG A 1106 |
Chain | Residue |
A | ASN1083 |
A | HOH1455 |
A | HOH1653 |
A | HOH1803 |
A | HOH2156 |
A | HOH2479 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GOL A 1107 |
Chain | Residue |
A | ASP758 |
A | SER759 |
A | ALA761 |
A | ARG764 |
A | GLN1069 |
A | HOH1203 |
A | HOH1228 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue GOL A 1108 |
Chain | Residue |
A | HIS653 |
A | LYS676 |
A | TYR741 |
A | ASN835 |
A | PHE836 |
A | HOH1220 |
A | HOH1367 |
site_id | AC9 |
Number of Residues | 11 |
Details | binding site for residue GOL A 1109 |
Chain | Residue |
A | VAL459 |
A | GLY460 |
A | ASN471 |
A | ASN473 |
A | ASN994 |
A | ARG997 |
A | HOH1246 |
A | HOH1307 |
A | HOH1633 |
A | HOH1694 |
A | HOH1780 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue GOL A 1110 |
Chain | Residue |
A | VAL352 |
A | HIS394 |
A | TYR411 |
A | ARG448 |
A | HOH1611 |
A | HOH1613 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue GOL A 1111 |
Chain | Residue |
A | VAL245 |
A | ASP247 |
A | PHE275 |
A | ILE330 |
A | HOH1210 |
A | HOH1403 |
A | HOH1588 |
A | HOH1879 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue GOL A 1112 |
Chain | Residue |
A | HOH1888 |
A | HOH1992 |
A | THR305 |
A | ARG325 |
A | GLU572 |
A | HOH1521 |
A | HOH1671 |
A | HOH1732 |
A | HOH1823 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue GOL A 1113 |
Chain | Residue |
A | LYS479 |
A | TYR880 |
A | VAL887 |
A | ASP888 |
A | GLN891 |
A | ARG895 |
A | TYR925 |
A | HOH1450 |
A | HOH1638 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue DMS A 1114 |
Chain | Residue |
A | ASN573 |
A | TYR575 |
A | HOH1603 |
A | HOH1753 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue PO4 A 1115 |
Chain | Residue |
A | ARG489 |
A | THR492 |
A | HIS496 |
A | GLU526 |
A | J6A1102 |
A | HOH1212 |
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 |