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5Y1Q

Crystal structure of Plasmodium falciparum aminopeptidase N in complex with (S)-2-(3-(3-chlorobenzyl)ureido)-N-hydroxy-4-methylpentanamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1101
ChainResidue
AHIS496
AHIS500
AGLU519
A8L01105

site_idAC2
Number of Residues7
Detailsbinding site for residue MG A 1102
ChainResidue
AHOH1431
AHOH1452
AGLY250
AGLU699
AHOH1201
AHOH1319
AHOH1384

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 1103
ChainResidue
AHOH1266
AHOH1299
AHOH1372
AHOH1486
AHOH1493
AHOH1494

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 1104
ChainResidue
AGLU526
AHOH1378
AHOH1380
AHOH1445
AHOH1461
AHOH1492

site_idAC5
Number of Residues14
Detailsbinding site for residue 8L0 A 1105
ChainResidue
AGLU319
AVAL459
AGLY460
AALA461
AMET462
AGLU463
AHIS496
AGLU497
AHIS500
AGLU519
ATYR575
ATYR580
AZN1101
AHOH1212

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVGHEYFHNY
ChainResidueDetails
AVAL493-TYR502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P15144
ChainResidueDetails
AGLU497

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:19196988, ECO:0000305|PubMed:21366301, ECO:0007744|PDB:3EBH, ECO:0007744|PDB:3EBI, ECO:0007744|PDB:3Q43
ChainResidueDetails
AGLU319
AGLY460
AGLU463

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:19196988, ECO:0000305|PubMed:21366301, ECO:0007744|PDB:3EBH, ECO:0007744|PDB:3Q43
ChainResidueDetails
AALA461

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19196988, ECO:0000269|PubMed:21366301, ECO:0000269|PubMed:21844374, ECO:0000269|PubMed:23713488, ECO:0000269|PubMed:23897806, ECO:0000269|PubMed:25299353, ECO:0000269|PubMed:25645579, ECO:0000269|PubMed:26406322, ECO:0000269|PubMed:26807544, ECO:0000269|PubMed:30537832, ECO:0000269|PubMed:32182520, ECO:0000269|Ref.21, ECO:0000269|DOI:10.1016/j.cclet.2021.09.102, ECO:0000312|PDB:3T8V, ECO:0000312|PDB:5Y1Q, ECO:0007744|PDB:3EBG, ECO:0007744|PDB:3EBH, ECO:0007744|PDB:3EBI, ECO:0007744|PDB:3Q43, ECO:0007744|PDB:3Q44, ECO:0007744|PDB:4J3B, ECO:0007744|PDB:4K5L, ECO:0007744|PDB:4K5M, ECO:0007744|PDB:4K5N, ECO:0007744|PDB:4K5O, ECO:0007744|PDB:4K5P, ECO:0007744|PDB:4R5T, ECO:0007744|PDB:4R5V, ECO:0007744|PDB:4R5X, ECO:0007744|PDB:4X2U, ECO:0007744|PDB:4ZQT, ECO:0007744|PDB:4ZW3, ECO:0007744|PDB:4ZW5, ECO:0007744|PDB:4ZW6, ECO:0007744|PDB:4ZW7, ECO:0007744|PDB:4ZW8, ECO:0007744|PDB:4ZX3, ECO:0007744|PDB:4ZX4, ECO:0007744|PDB:4ZX5, ECO:0007744|PDB:4ZX6, ECO:0007744|PDB:5XM7, ECO:0007744|PDB:5Y19, ECO:0007744|PDB:5Y1H, ECO:0007744|PDB:5Y1K, ECO:0007744|PDB:5Y1R, ECO:0007744|PDB:5Y1S, ECO:0007744|PDB:5Y1T, ECO:0007744|PDB:5Y1V, ECO:0007744|PDB:5Y1W, ECO:0007744|PDB:5Y1X, ECO:0007744|PDB:5Y3I, ECO:0007744|PDB:6EA1, ECO:0007744|PDB:6EA2, ECO:0007744|PDB:6EAA, ECO:0007744|PDB:6EAB, ECO:0007744|PDB:6EE3, ECO:0007744|PDB:6EE4, ECO:0007744|PDB:6EE6, ECO:0007744|PDB:6EED, ECO:0007744|PDB:6SBQ, ECO:0007744|PDB:6SBR
ChainResidueDetails
AHIS496
AHIS500
AGLU519

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for substrate specificity => ECO:0000269|PubMed:23897806
ChainResidueDetails
AVAL459

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P15144
ChainResidueDetails
ATYR580

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Cleavage => ECO:0000305|PubMed:21659511
ChainResidueDetails
AASN795

220472

PDB entries from 2024-05-29

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