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4CEJ

Crystal structure of AddAB-DNA-ADPNP complex at 3 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000724biological_processdouble-strand break repair via homologous recombination
A0000725biological_processrecombinational repair
A0003677molecular_functionDNA binding
A0003678molecular_functionDNA helicase activity
A0003690molecular_functiondouble-stranded DNA binding
A0004386molecular_functionhelicase activity
A0004527molecular_functionexonuclease activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006302biological_processdouble-strand break repair
A0008408molecular_function3'-5' exonuclease activity
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0032508biological_processDNA duplex unwinding
A0033202cellular_componentDNA helicase complex
A0043138molecular_function3'-5' DNA helicase activity
B0000724biological_processdouble-strand break repair via homologous recombination
B0003677molecular_functionDNA binding
B0003690molecular_functiondouble-stranded DNA binding
B0004386molecular_functionhelicase activity
B0004527molecular_functionexonuclease activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0006281biological_processDNA repair
B0006310biological_processDNA recombination
B0008409molecular_function5'-3' exonuclease activity
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ANP A 2233
ChainResidue
ATHR10
AALA38
AGLN441
APHE478
AARG479
ALYS573
AGLU800
AARG873
AHOH2001
AHOH2002
AHOH2003
AGLN15
AMG2234
AALA31
AALA32
AGLY33
ASER34
AGLY35
ALYS36
ATHR37

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 2234
ChainResidue
ATHR37
AHOH2001
AHOH2002
AHOH2003
AANP2233

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SF4 B 2160
ChainResidue
BCYS801
BPRO1112
BCYS1121
BCYS1124
BCYS1130

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ANP B 2161
ChainResidue
BSER10
BGLY11
BSER12
BGLY13
BLYS14
BTHR15
BLYS16
BTHR236
BGLU282
BARG283
BGLY600
BMET656
BHOH2001
BHOH2002
BMG2162

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 2162
ChainResidue
BTHR15
BASP208
BHOH2001
BHOH2002
BHOH2003
BANP2161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ
ChainResidueDetails
BSER10
BGLY11
BLYS16
BTHR236

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:24670664, ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ
ChainResidueDetails
BLYS14
BTHR15
BARG283
AARG479
AARG873

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01452, ECO:0000269|PubMed:22307084, ECO:0000269|PubMed:24670664, ECO:0007744|PDB:3U44, ECO:0007744|PDB:4CEH, ECO:0007744|PDB:4CEI, ECO:0007744|PDB:4CEJ
ChainResidueDetails
BCYS801
BCYS1121
BCYS1124
BCYS1130

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PDB entries from 2024-10-30

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