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4JCV

Crystal structure of the RecOR complex in an open conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000725biological_processrecombinational repair
A0003677molecular_functionDNA binding
A0006281biological_processDNA repair
A0006302biological_processdouble-strand break repair
A0006310biological_processDNA recombination
A0006974biological_processDNA damage response
A0008270molecular_functionzinc ion binding
A0046872molecular_functionmetal ion binding
B0000725biological_processrecombinational repair
B0003677molecular_functionDNA binding
B0006281biological_processDNA repair
B0006302biological_processdouble-strand break repair
B0006310biological_processDNA recombination
B0006974biological_processDNA damage response
B0008270molecular_functionzinc ion binding
B0046872molecular_functionmetal ion binding
C0000725biological_processrecombinational repair
C0003677molecular_functionDNA binding
C0006281biological_processDNA repair
C0006302biological_processdouble-strand break repair
C0006310biological_processDNA recombination
C0006974biological_processDNA damage response
C0008270molecular_functionzinc ion binding
C0046872molecular_functionmetal ion binding
D0000725biological_processrecombinational repair
D0003677molecular_functionDNA binding
D0006281biological_processDNA repair
D0006302biological_processdouble-strand break repair
D0006310biological_processDNA recombination
D0006974biological_processDNA damage response
D0008270molecular_functionzinc ion binding
D0046872molecular_functionmetal ion binding
E0006281biological_processDNA repair
E0006302biological_processdouble-strand break repair
E0006310biological_processDNA recombination
E0006974biological_processDNA damage response
E0043590cellular_componentbacterial nucleoid
E0046872molecular_functionmetal ion binding
F0006281biological_processDNA repair
F0006302biological_processdouble-strand break repair
F0006310biological_processDNA recombination
F0006974biological_processDNA damage response
F0043590cellular_componentbacterial nucleoid
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS57
ACYS60
ACYS69
ACYS72

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BCYS57
BCYS60
BCYS69
BCYS72

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 301
ChainResidue
CCYS60
CCYS69
CCYS72
CCYS57

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
DCYS57
DCYS60
DCYS69
DCYS72

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 301
ChainResidue
ECYS153
ECYS156
ECYS173
ECYS176

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 301
ChainResidue
FCYS153
FCYS156
FCYS173
FCYS176

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Ewval.VMSYKLLGL
ChainResidueDetails
EGLU130-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 Residues372
DetailsDomain: {"description":"Toprim","evidences":[{"source":"HAMAP-Rule","id":"MF_00017","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues60
DetailsZinc finger: {"description":"C4-type","evidences":[{"source":"HAMAP-Rule","id":"MF_00017","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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