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2V1C

Crystal structure and mutational study of RecOR provide insight into its role in DNA repair

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0006281biological_processDNA repair
A0006302biological_processdouble-strand break repair
A0006310biological_processDNA recombination
A0046872molecular_functionmetal ion binding
B0003677molecular_functionDNA binding
B0006281biological_processDNA repair
B0006302biological_processdouble-strand break repair
B0006310biological_processDNA recombination
B0046872molecular_functionmetal ion binding
C0006281biological_processDNA repair
C0006302biological_processdouble-strand break repair
C0006310biological_processDNA recombination
C0043590cellular_componentbacterial nucleoid
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 230
ChainResidue
ACYS57
ACYS60
ACYS69
ACYS72

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 230
ChainResidue
BCYS57
BCYS60
BCYS69
BCYS72

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 266
ChainResidue
CCYS156
CCYS173
CCYS176
CCYS153

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Ewval.VMSYKLLGL
ChainResidueDetails
CGLU130-LEU143

site_idPS01300
Number of Residues22
DetailsRECR RecR protein signature. CpiCfni..TdaekCdVCadpsRD
ChainResidueDetails
ACYS57-ASP78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsZN_FING: C4-type => ECO:0000255|HAMAP-Rule:MF_00017
ChainResidueDetails
ACYS57-CYS72
BCYS57-CYS72

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PDB entries from 2024-07-17

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