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2VF7

Crystal structure of UvrA2 from Deinococcus radiodurans

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003677molecular_functionDNA binding
A0004518molecular_functionnuclease activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006289biological_processnucleotide-excision repair
A0006974biological_processDNA damage response
A0008270molecular_functionzinc ion binding
A0009380cellular_componentexcinuclease repair complex
A0016887molecular_functionATP hydrolysis activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003677molecular_functionDNA binding
B0004518molecular_functionnuclease activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006281biological_processDNA repair
B0006289biological_processnucleotide-excision repair
B0006974biological_processDNA damage response
B0008270molecular_functionzinc ion binding
B0009380cellular_componentexcinuclease repair complex
B0016887molecular_functionATP hydrolysis activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0003677molecular_functionDNA binding
C0004518molecular_functionnuclease activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006281biological_processDNA repair
C0006289biological_processnucleotide-excision repair
C0006974biological_processDNA damage response
C0008270molecular_functionzinc ion binding
C0009380cellular_componentexcinuclease repair complex
C0016887molecular_functionATP hydrolysis activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ADP A 901
ChainResidue
ATYR370
ASER537
ATHR538
AGLY810
AARG375
AASN511
AASN512
AVAL531
AGLY533
ASER534
AGLY535
ALYS536

site_idAC2
Number of Residues18
Detailsbinding site for residue ADP A 902
ChainResidue
AHIS24
AASN25
AVAL44
AGLY46
ASER47
AGLY48
ALYS49
ASER50
ASER51
AARG101
AGLN726
AGLU730
AHOH1001
AHOH1045
AHOH1063
AHOH1066
AHOH1088
AHOH1098

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 903
ChainResidue
ACYS151
ACYS154
ACYS287
ACYS290

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 904
ChainResidue
ACYS641
ACYS644
ACYS664
ACYS667

site_idAC5
Number of Residues14
Detailsbinding site for residue ADP B 901
ChainResidue
BTYR370
BARG375
BASN511
BASN512
BVAL531
BGLY533
BSER534
BGLY535
BLYS536
BSER537
BTHR538
BHOH1037
BHOH1113
BHOH1137

site_idAC6
Number of Residues14
Detailsbinding site for residue ADP B 902
ChainResidue
BHIS24
BASN25
BVAL44
BGLY46
BSER47
BGLY48
BLYS49
BSER50
BSER51
BARG101
BGLN726
BGLU730
BHOH1002
BHOH1028

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 903
ChainResidue
BCYS151
BCYS154
BCYS287
BCYS290

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 904
ChainResidue
BCYS641
BCYS644
BCYS664
BCYS667

site_idAC9
Number of Residues16
Detailsbinding site for residue ADP C 901
ChainResidue
CTYR370
CARG375
CASN511
CASN512
CSER532
CGLY533
CSER534
CGLY535
CLYS536
CSER537
CTHR538
CGLY810
CHOH1007
CHOH1012
CHOH1025
CHOH1040

site_idAD1
Number of Residues18
Detailsbinding site for residue ADP C 902
ChainResidue
CSER51
CARG101
CLEU722
CGLN726
CGLU730
CMG905
CHOH1019
CHOH1034
CHOH1116
CHIS24
CASN25
CVAL44
CSER45
CGLY46
CSER47
CGLY48
CLYS49
CSER50

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN C 903
ChainResidue
CCYS151
CCYS154
CCYS287
CCYS290

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN C 904
ChainResidue
CCYS641
CCYS644
CCYS664
CCYS667

site_idAD4
Number of Residues3
Detailsbinding site for residue MG C 905
ChainResidue
CARG101
CGLU735
CADP902

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSPGELQRLRLATQL
ChainResidueDetails
ALEU380-LEU394
ALEU731-LEU745

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PDB entries from 2025-12-17

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