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4RGZ

Crystal structure of recombinant prolidase from Thermococcus sibiricus at P21221 spacegroup

Functional Information from GO Data
ChainGOidnamespacecontents
10004177molecular_functionaminopeptidase activity
10046872molecular_functionmetal ion binding
A0004177molecular_functionaminopeptidase activity
A0046872molecular_functionmetal ion binding
e0004177molecular_functionaminopeptidase activity
e0046872molecular_functionmetal ion binding
N0004177molecular_functionaminopeptidase activity
N0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AASP229
AASP240
ATHR242
AGLU333
AGLU347
AHOH518

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AARG301
AHIS304

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN N 401
ChainResidue
NZN402
NHOH548
NASP229

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN N 402
ChainResidue
NASP229
NASP240
NTHR242
NGLU347
NZN401
NHOH548

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN 1 401
ChainResidue
1ASP229
1ASP240
1THR242
1GLU347
1ZN404

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 1 402
ChainResidue
1HIS212
1ARG301
1HIS304
1HIS311
1GLU333
1ZN404
1HOH515
eARG49

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 1 403
ChainResidue
1SER175
1GLU178
1HIS217
1LYS219
1HOH519

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN 1 404
ChainResidue
1ASP229
1GLU333
1ZN401
1PO4402
1HOH511

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 1 405
ChainResidue
1ASN210
1HIS213
eGLU72

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN e 401
ChainResidue
eASP229
eASP240
eTHR242
eGLU347
eZN402

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN e 402
ChainResidue
eASP240
eHIS304
eGLU333
eGLU347
eZN401

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HRTGHgLGIdVHE
ChainResidueDetails
AHIS300-GLU312

225946

PDB entries from 2024-10-09

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