4R5X
Structure of the m1 alanylaminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor
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 | R5X1107 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 1102 |
Chain | Residue |
A | ARG997 |
A | HOH1201 |
A | HOH1692 |
A | VAL459 |
A | ASN471 |
A | ASN473 |
A | SER474 |
A | ARG489 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 1103 |
Chain | Residue |
A | MET533 |
A | THR534 |
A | VAL887 |
A | ASP888 |
A | PHE889 |
A | ASP890 |
A | DMS1112 |
A | HOH1560 |
A | HOH1947 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1104 |
Chain | Residue |
A | TYR575 |
A | THR576 |
A | THR577 |
A | TYR580 |
A | ASP581 |
A | R5X1107 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1105 |
Chain | Residue |
A | GLY250 |
A | HOH1357 |
A | HOH1400 |
A | HOH1483 |
A | HOH1484 |
A | HOH2034 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 1106 |
Chain | Residue |
A | LYS479 |
A | TYR880 |
A | VAL887 |
A | ASP888 |
A | GLN891 |
A | ARG895 |
A | TYR925 |
A | HOH1210 |
A | HOH1280 |
site_id | AC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE R5X A 1107 |
Chain | Residue |
A | GLU319 |
A | VAL459 |
A | GLY460 |
A | ALA461 |
A | MET462 |
A | GLU463 |
A | ARG489 |
A | HIS496 |
A | GLU497 |
A | HIS500 |
A | GLU519 |
A | TYR575 |
A | TYR580 |
A | MET1034 |
A | ZN1101 |
A | GOL1104 |
A | HOH1601 |
A | HOH1692 |
A | HOH1775 |
A | HOH2029 |
A | HOH2032 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 1108 |
Chain | Residue |
A | ASN573 |
A | THR1037 |
A | TYR1077 |
A | HOH1335 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 1109 |
Chain | Residue |
A | TYR853 |
A | SER903 |
A | LYS907 |
A | DMS1110 |
A | HOH1315 |
A | HOH1362 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 1110 |
Chain | Residue |
A | VAL825 |
A | SER826 |
A | TYR853 |
A | SER903 |
A | DMS1109 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 1111 |
Chain | Residue |
A | VAL245 |
A | ASP247 |
A | PHE275 |
A | HOH1766 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 1112 |
Chain | Residue |
A | HIS886 |
A | VAL887 |
A | ASP888 |
A | GOL1103 |
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 |