6EE4
X-ray crystal structure of Pf-M1 in complex with inhibitor (6m) 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 | J4S1102 |
site_id | AC2 |
Number of Residues | 19 |
Details | binding site for residue J4S 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 | TYR580 |
A | MET1034 |
A | ZN1101 |
A | PO41109 |
A | THR305 |
A | GLN317 |
A | GLU319 |
A | ALA320 |
A | ASN458 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue GOL A 1103 |
Chain | Residue |
A | VAL459 |
A | ASN471 |
A | ASN473 |
A | SER474 |
A | ARG489 |
A | ASN994 |
A | ARG997 |
A | HOH1321 |
A | HOH1678 |
A | HOH1950 |
A | HOH2079 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue GOL A 1104 |
Chain | Residue |
A | ALA303 |
A | THR305 |
A | ARG325 |
A | GLU572 |
A | HOH1373 |
A | HOH1454 |
A | HOH1532 |
A | HOH1758 |
A | HOH1967 |
A | HOH2022 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue GOL A 1105 |
Chain | Residue |
A | LYS479 |
A | TYR880 |
A | VAL887 |
A | ASP888 |
A | GLN891 |
A | ARG895 |
A | TYR925 |
A | HOH1679 |
A | HOH1695 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue GOL A 1106 |
Chain | Residue |
A | ASN573 |
A | TYR575 |
A | THR1037 |
A | GLN1038 |
A | TYR1077 |
A | HOH1262 |
A | HOH1352 |
A | HOH1627 |
A | HOH1935 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue GOL A 1107 |
Chain | Residue |
A | ASP545 |
A | TYR765 |
A | CYS768 |
A | THR769 |
A | TYR772 |
A | TYR823 |
A | SER826 |
A | PRO828 |
A | HOH1215 |
A | HOH1619 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue PO4 A 1108 |
Chain | Residue |
A | ASN273 |
A | GLU699 |
A | ASN700 |
A | TYR757 |
A | HOH1239 |
A | HOH1575 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue PO4 A 1109 |
Chain | Residue |
A | ARG489 |
A | HIS496 |
A | GLU497 |
A | GLU526 |
A | J4S1102 |
A | HOH1411 |
A | HOH1910 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue PO4 A 1110 |
Chain | Residue |
A | HIS653 |
A | LYS676 |
A | TYR741 |
A | ASN835 |
A | PHE836 |
A | HOH1202 |
A | HOH1320 |
A | HOH1457 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue MG A 1111 |
Chain | Residue |
A | HOH2566 |
A | GLU957 |
A | HOH1404 |
A | HOH1621 |
A | HOH1804 |
A | HOH2329 |
A | HOH2539 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue MG A 1112 |
Chain | Residue |
A | HOH1586 |
A | HOH1658 |
A | HOH1862 |
A | HOH2264 |
A | HOH2504 |
A | HOH2679 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue MG A 1113 |
Chain | Residue |
A | THR492 |
A | GLU526 |
A | HOH1699 |
A | HOH1856 |
A | HOH1910 |
A | HOH2069 |
A | HOH2461 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue MG A 1114 |
Chain | Residue |
A | GLY250 |
A | HOH1575 |
A | HOH1661 |
A | HOH1819 |
A | HOH2014 |
A | HOH2388 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue MG A 1115 |
Chain | Residue |
A | ASN1083 |
A | HOH1366 |
A | HOH1680 |
A | HOH1778 |
A | HOH2160 |
A | HOH2554 |
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 |