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1U98

Crystal Structure of E. coli RecA in a Compressed Helical Filament Form3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000725biological_processrecombinational repair
A0003677molecular_functionDNA binding
A0003684molecular_functiondamaged DNA binding
A0003697molecular_functionsingle-stranded DNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006259biological_processDNA metabolic process
A0006281biological_processDNA repair
A0006310biological_processDNA recombination
A0006974biological_processDNA damage response
A0008094molecular_functionATP-dependent activity, acting on DNA
A0009355cellular_componentDNA polymerase V complex
A0009432biological_processSOS response
A0010212biological_processresponse to ionizing radiation
A0016887molecular_functionATP hydrolysis activity
A0019985biological_processtranslesion synthesis
A0035825biological_processhomologous recombination
A0048870biological_processcell motility
A0140297molecular_functionDNA-binding transcription factor binding
A0140664molecular_functionATP-dependent DNA damage sensor activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
APRO67
AGLU68
ASER69
ASER70
AGLY71
ALYS72
ATHR73
AHOH533

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
AALA147
ATHR208
ALYS216
AHOH411
AHOH502
AHOH530
AGLU96

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
AARG60
AASP120
APHE217
ATYR218
ALYS250
AHOH450
AHOH505

Functional Information from PROSITE/UniProt
site_idPS00321
Number of Residues9
DetailsRECA_1 recA signature. ALKFYASVR
ChainResidueDetails
AALA214-ARG222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00268, ECO:0000269|PubMed:1731253
ChainResidueDetails
APRO67

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PDB entries from 2024-06-12

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