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2IW2

Crystal structure of human Prolidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0005515molecular_functionprotein binding
A0006508biological_processproteolysis
A0006520biological_processamino acid metabolic process
A0008233molecular_functionpeptidase activity
A0008235molecular_functionmetalloexopeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0016805molecular_functiondipeptidase activity
A0030145molecular_functionmanganese ion binding
A0030574biological_processcollagen catabolic process
A0043069biological_processnegative regulation of programmed cell death
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
A0070062cellular_componentextracellular exosome
A0102009molecular_functionproline dipeptidase activity
B0004181molecular_functionmetallocarboxypeptidase activity
B0005515molecular_functionprotein binding
B0006508biological_processproteolysis
B0006520biological_processamino acid metabolic process
B0008233molecular_functionpeptidase activity
B0008235molecular_functionmetalloexopeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0016787molecular_functionhydrolase activity
B0016805molecular_functiondipeptidase activity
B0030145molecular_functionmanganese ion binding
B0030574biological_processcollagen catabolic process
B0043069biological_processnegative regulation of programmed cell death
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
B0070062cellular_componentextracellular exosome
B0102009molecular_functionproline dipeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A1484
ChainResidue
AASP288
AHIS371
AGLU413
AGLU453
ANA1485
AHOH2404

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A1485
ChainResidue
ANA1484
AASP277
AASP288
AGLU453

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A1486
ChainResidue
AGLY319
AHOH2362
AHOH2470
BALA40

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B1484
ChainResidue
BASP277
BASP288
BGLU453
BNA1485
BHOH2361

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B1485
ChainResidue
BASP288
BHIS371
BGLU413
BGLU453
BNA1484
BHOH2417

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLGHfLGIdVHD
ChainResidueDetails
AHIS367-ASP379

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28677335","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5M4J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5M4L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28677335","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5M4G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5M4L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5M4Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU413
AHIS378

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BGLU413
BHIS378

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU413

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BGLU413

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PDB entries from 2025-12-24

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