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2R6F

Crystal Structure of Bacillus stearothermophilus UvrA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0004518molecular_functionnuclease activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006289biological_processnucleotide-excision repair
A0008270molecular_functionzinc ion binding
A0009380cellular_componentexcinuclease repair complex
A0009381molecular_functionexcinuclease ABC activity
A0009432biological_processSOS response
A0016887molecular_functionATP hydrolysis activity
A0046872molecular_functionmetal ion binding
B0003677molecular_functionDNA binding
B0003824molecular_functioncatalytic activity
B0004518molecular_functionnuclease activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006281biological_processDNA repair
B0006289biological_processnucleotide-excision repair
B0008270molecular_functionzinc ion binding
B0009380cellular_componentexcinuclease repair complex
B0009381molecular_functionexcinuclease ABC activity
B0009432biological_processSOS response
B0016887molecular_functionATP hydrolysis activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP A 1000
ChainResidue
AHIS12
ATYR816
AMSE817
AGLN821
AHOH1007
AASN13
ALEU32
AGLY34
ASER35
AGLY36
ALYS37
ASER38
ASER39

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP A 1001
ChainResidue
ATYR475
AARG480
AHIS618
AASN619
AVAL638
AGLY640
ASER641
AGLY642
ALYS643
ASER644
ATHR645
AHOH1008

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1004
ChainResidue
ACYS120
AHIS123
ACYS250
ACYS253

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1005
ChainResidue
ACYS274
ACYS277
ACYS404
ACYS407

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1006
ChainResidue
ACYS736
ACYS739
ACYS759
ACYS762

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP B 1002
ChainResidue
BHIS12
BLEU32
BGLY34
BSER35
BGLY36
BLYS37
BSER38
BSER39
BGLY563
BTYR816
BGLN821
BTHR825

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP B 1003
ChainResidue
BTYR475
BARG480
BHIS618
BASN619
BVAL638
BSER639
BGLY640
BSER641
BGLY642
BLYS643
BSER644
BTHR645
BGLY905
BHOH1011

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1007
ChainResidue
BCYS120
BHIS123
BCYS250
BCYS253

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1008
ChainResidue
BCYS274
BCYS277
BCYS404
BCYS407

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1009
ChainResidue
BCYS736
BCYS739
BCYS759
BCYS762

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGEAQRIRLATQI
ChainResidueDetails
ALEU485-ILE499
ALEU826-LEU840

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PDB entries from 2024-10-09

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