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6XMR

X-ray crystallographic structure model of Lactococcus lactis prolidase mutant H38S

Functional Information from GO Data
ChainGOidnamespacecontents
A0016805molecular_functiondipeptidase activity
A0046872molecular_functionmetal ion binding
A0102009molecular_functionproline dipeptidase activity
B0016805molecular_functiondipeptidase activity
B0046872molecular_functionmetal ion binding
B0102009molecular_functionproline dipeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MN A 401
ChainResidue
AASP232
AHIS296
AGLU325
AGLU339
AMN402
AHOH521
AHOH730

site_idAC2
Number of Residues7
Detailsbinding site for residue MN A 402
ChainResidue
ATHR234
AGLU339
AMN401
AHOH521
AHOH831
AASP221
AASP232

site_idAC3
Number of Residues7
Detailsbinding site for residue MN B 401
ChainResidue
BASP221
BASP232
BTHR234
BGLU339
BMN402
BHOH544
BHOH866

site_idAC4
Number of Residues7
Detailsbinding site for residue MN B 402
ChainResidue
BASP232
BHIS296
BGLU325
BGLU339
BMN401
BHOH544
BHOH658

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HRLGHgIGMdVHE
ChainResidueDetails
AHIS292-GLU304

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PDB entries from 2024-06-12

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