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3CTZ

Structure of human cytosolic X-prolyl aminopeptidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0010815biological_processbradykinin catabolic process
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0042803molecular_functionprotein homodimerization activity
A0043069biological_processnegative regulation of programmed cell death
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 624
ChainResidue
AASP426
AHIS489
AGLU523
AGLU537
AHOH644
AHOH1519
AHOH1520

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 625
ChainResidue
AASP426
ATHR428
AGLU537
AHOH644
AHOH1518
APHE381
AASP415

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 626
ChainResidue
AASP281
ATHR435
AHOH658
AHOH670
AHOH717
AHOH739
AHOH752

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 627
ChainResidue
AGLY486
ALYS507

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE P6G A 628
ChainResidue
APHE381
AILE394
AHIS395
AHIS485
AGLY486
AHIS489
AHIS498
AGLU523
AHOH659
AHOH792
AHOH861
AHOH1298
AHOH1518
AHOH1520

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGTGHgVGSfLNV
ChainResidueDetails
AHIS485-VAL497

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O44750","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18515364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CTZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU523
APRO501

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU523

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU523
AHIS498

246704

PDB entries from 2025-12-24

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