5XM7
Crystal structure of Plasmodium falciparum aminopeptidase N in complex with (S)-2-((2S,3R)-3-amino-2-hydroxy-4-phenylbutanamido)-N-hydroxy-4-methylpentanamide
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 | 89X1116 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue MG A 1102 |
Chain | Residue |
A | HOH1484 |
A | HOH1513 |
A | GLY250 |
A | GLU699 |
A | HOH1210 |
A | HOH1240 |
A | HOH1311 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue MG A 1103 |
Chain | Residue |
A | GLU957 |
A | GOL1109 |
A | HOH1214 |
A | HOH1384 |
A | HOH1411 |
A | HOH1486 |
A | HOH1564 |
A | HOH1575 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG A 1104 |
Chain | Residue |
A | HOH1282 |
A | HOH1290 |
A | HOH1385 |
A | HOH1551 |
A | HOH1570 |
A | HOH1578 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 1105 |
Chain | Residue |
A | TYR853 |
A | SER903 |
A | LEU904 |
A | LYS907 |
A | HOH1389 |
A | HOH1402 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL A 1106 |
Chain | Residue |
A | ASN659 |
A | GLN666 |
A | SER668 |
A | PHE783 |
A | LEU796 |
A | TYR851 |
A | GOL1107 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue GOL A 1107 |
Chain | Residue |
A | LYS657 |
A | TYR658 |
A | ASN659 |
A | SER668 |
A | HIS670 |
A | TYR851 |
A | LYS854 |
A | GLN855 |
A | GOL1106 |
A | HOH1442 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue GOL A 1108 |
Chain | Residue |
A | SER921 |
A | LYS922 |
A | SER923 |
A | PRO924 |
A | TRP929 |
A | LEU952 |
A | HOH1474 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue GOL A 1109 |
Chain | Residue |
A | LEU960 |
A | VAL986 |
A | LEU987 |
A | ASP995 |
A | MG1103 |
A | HOH1214 |
A | HOH1272 |
A | HOH1486 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue GOL A 1110 |
Chain | Residue |
A | VAL459 |
A | GLY460 |
A | ASN471 |
A | ASN473 |
A | ARG997 |
A | GLN1038 |
A | HOH1223 |
A | HOH1336 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue GOL A 1111 |
Chain | Residue |
A | VAL245 |
A | ASP247 |
A | PHE275 |
A | ILE330 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue GOL A 1112 |
Chain | Residue |
A | GLN673 |
A | TYR674 |
A | THR675 |
A | LYS684 |
A | LYS685 |
A | PRO686 |
A | GLU715 |
A | HOH1225 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 1113 |
Chain | Residue |
A | HIS653 |
A | TYR741 |
A | ASN835 |
A | PHE836 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue GOL A 1114 |
Chain | Residue |
A | LYS281 |
A | LEU777 |
A | PHE836 |
A | VAL837 |
A | SER838 |
A | HOH1226 |
A | HOH1395 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue GOL A 1115 |
Chain | Residue |
A | THR215 |
A | THR879 |
A | TYR880 |
A | HOH1299 |
site_id | AD7 |
Number of Residues | 14 |
Details | binding site for residue 89X A 1116 |
Chain | Residue |
A | VAL459 |
A | GLY460 |
A | ALA461 |
A | GLU463 |
A | HIS496 |
A | GLU497 |
A | HIS500 |
A | GLU519 |
A | TYR575 |
A | TYR580 |
A | ZN1101 |
A | HOH1208 |
A | HOH1372 |
A | GLU319 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVGHEYFHNY |
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 | ASN795 |