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1WN1

Crystal Structure of Dipeptiase from Pyrococcus Horikoshii OT3

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 1001
ChainResidue
AASP226
AHIS290
AGLU319
AGLU333
ACO1003

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 1002
ChainResidue
BCO1004
BASP226
BHIS290
BGLU319
BGLU333

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 1003
ChainResidue
AASP215
AASP226
AILE227
ATHR228
AGLU333
ACO1001

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO B 1004
ChainResidue
BASP215
BASP226
BILE227
BTHR228
BGLU333
BCO1002

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HRTGHgLGLdVHE
ChainResidueDetails
AHIS286-GLU298

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU319
AHIS297

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BGLU319
BHIS297

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU319

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
BGLU319

225681

PDB entries from 2024-10-02

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