5Y1K
Crystal structure of Plasmodium falciparum aminopeptidase N in complex with (S)-2-(3-(2-chlorobenzyl)ureido)-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 | B1B1111 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 1102 |
Chain | Residue |
A | HOH1652 |
A | GLY250 |
A | HOH1278 |
A | HOH1292 |
A | HOH1584 |
A | HOH1588 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue MG A 1103 |
Chain | Residue |
A | GLU526 |
A | GOL1107 |
A | HOH1207 |
A | HOH1238 |
A | HOH1410 |
A | HOH1585 |
A | HOH1623 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG A 1104 |
Chain | Residue |
A | HOH1300 |
A | HOH1406 |
A | HOH1442 |
A | HOH1638 |
A | HOH1655 |
A | HOH1658 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue GOL A 1105 |
Chain | Residue |
A | MET533 |
A | THR534 |
A | LYS535 |
A | HIS886 |
A | VAL887 |
A | ASP888 |
A | PHE889 |
A | ASP890 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 1106 |
Chain | Residue |
A | GLU572 |
A | ASN573 |
A | TYR575 |
A | THR1037 |
A | GLN1038 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue GOL A 1107 |
Chain | Residue |
A | ALA461 |
A | ARG489 |
A | VAL493 |
A | HIS496 |
A | GLU497 |
A | MG1103 |
A | B1B1111 |
A | HOH1207 |
A | HOH1238 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL A 1108 |
Chain | Residue |
A | TYR853 |
A | SER903 |
A | LYS907 |
A | HOH1229 |
A | HOH1253 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue GOL A 1109 |
Chain | Residue |
A | GLN673 |
A | TYR674 |
A | THR675 |
A | LYS684 |
A | LYS685 |
A | PRO686 |
A | GLU715 |
A | HOH1318 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue GOL A 1110 |
Chain | Residue |
A | ASN659 |
A | ASP661 |
A | GLN666 |
A | SER668 |
A | PHE783 |
site_id | AD2 |
Number of Residues | 18 |
Details | binding site for residue B1B A 1111 |
Chain | Residue |
A | GLU319 |
A | ALA320 |
A | VAL459 |
A | GLY460 |
A | ALA461 |
A | GLU463 |
A | HIS496 |
A | GLU497 |
A | HIS500 |
A | GLU519 |
A | GLU572 |
A | TYR580 |
A | MET1034 |
A | ZN1101 |
A | GOL1107 |
A | HOH1212 |
A | HOH1218 |
A | HOH1624 |
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 |