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1WY2

Crystal Structure of the Prolidase from Pyrococcus horikoshii OT3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0016805molecular_functiondipeptidase activity
A0046872molecular_functionmetal ion binding
A0102009molecular_functionproline dipeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0016805molecular_functiondipeptidase activity
B0046872molecular_functionmetal ion binding
B0102009molecular_functionproline dipeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CAC A 403
ChainResidue
APHE181
AASP212
AASP223
AHIS294
AGLU316
AGLU330
AZN405
AZN406
AHOH1743

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CAC B 404
ChainResidue
BPHE181
BASP212
BASP223
BVAL293
BHIS294
BGLU316
BGLU330
BZN407
BZN408
BHOH548

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 405
ChainResidue
AASP212
AASP223
ATHR225
AGLU330
ACAC403
AZN406

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 406
ChainResidue
AASP223
AHIS287
AGLU316
AGLU330
ACAC403
AZN405

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 407
ChainResidue
BASP212
BASP223
BTHR225
BGLU330
BCAC404
BZN408

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 408
ChainResidue
BASP223
BHIS287
BGLU316
BGLU330
BCAC404
BZN407

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1409
ChainResidue
AHOH1424
AHOH1518
AHOH1613
AHOH1647
AHOH1746
AHOH1747

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1401
ChainResidue
ALYS27
AASN30
AGLU94
ASER95
ASER96
AASP118
AARG125
ATRP296
AGOL1402
AHOH1491

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1402
ChainResidue
ALYS27
AARG125
AGLU292
ATRP296
AGOL1401
AHOH1717

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HSLGHgVGLeVHE
ChainResidueDetails
AHIS283-GLU295

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AASP212
AASP223
BASP223
BHIS287
BGLU316
BGLU330
AHIS287
AGLU316
AGLU330
BASP212

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PDB entries from 2024-06-12

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