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5JQK

The Xray Crystal Structure of P. falciparum Aminopeptidase P

Functional Information from GO Data
ChainGOidnamespacecontents
A0070006molecular_functionmetalloaminopeptidase activity
B0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 801
ChainResidue
AASP581
AHIS644
AGLU676
AGLU690
AMN802
APO4803

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 802
ChainResidue
AGLU690
AMN801
APO4803
AASP570
AASP581
ATHR583

site_idAC3
Number of Residues8
Detailsbinding site for residue PO4 A 803
ChainResidue
AASP570
AASP581
AHIS644
AHIS653
AGLU676
AGLU690
AMN801
AMN802

site_idAC4
Number of Residues6
Detailsbinding site for residue MN B 801
ChainResidue
BASP581
BHIS644
BGLU676
BGLU690
BMN802
BPO4803

site_idAC5
Number of Residues6
Detailsbinding site for residue MN B 802
ChainResidue
BASP570
BASP581
BTHR583
BGLU690
BMN801
BPO4803

site_idAC6
Number of Residues9
Detailsbinding site for residue PO4 B 803
ChainResidue
BASP570
BASP581
BHIS644
BHIS653
BGLU676
BGLU690
BMN801
BMN802
BHOH974

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGTGHgVGLtLNV
ChainResidueDetails
AHIS640-VAL652

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27462122","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5JR6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27462122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5JQK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JR6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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