Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1HQC

STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8

Functional Information from GO Data
ChainGOidnamespacecontents
A0000400molecular_functionfour-way junction DNA binding
A0003677molecular_functionDNA binding
A0003689molecular_functionDNA clamp loader activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006310biological_processDNA recombination
A0006338biological_processchromatin remodeling
A0009378molecular_functionfour-way junction helicase activity
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0032508biological_processDNA duplex unwinding
A0036121molecular_functiondouble-stranded DNA helicase activity
A0048476cellular_componentHolliday junction resolvase complex
A0061749molecular_functionforked DNA-dependent helicase activity
A0061775molecular_functioncohesin loader activity
A0140584molecular_functionchromatin extrusion motor activity
A0140588biological_processchromatin looping
A0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
A0140849molecular_functionATP-dependent H2AZ histone chaperone activity
A1990518molecular_functionsingle-stranded 3'-5' DNA helicase activity
B0000400molecular_functionfour-way junction DNA binding
B0003677molecular_functionDNA binding
B0003689molecular_functionDNA clamp loader activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006281biological_processDNA repair
B0006310biological_processDNA recombination
B0006338biological_processchromatin remodeling
B0009378molecular_functionfour-way junction helicase activity
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0032508biological_processDNA duplex unwinding
B0036121molecular_functiondouble-stranded DNA helicase activity
B0048476cellular_componentHolliday junction resolvase complex
B0061749molecular_functionforked DNA-dependent helicase activity
B0061775molecular_functioncohesin loader activity
B0140584molecular_functionchromatin extrusion motor activity
B0140588biological_processchromatin looping
B0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
B0140849molecular_functionATP-dependent H2AZ histone chaperone activity
B1990518molecular_functionsingle-stranded 3'-5' DNA helicase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
ATHR52

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BVAL68

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ADE A 501
ChainResidue
ATYR14
AILE15
ATHR53
AARG179
ALYS208

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ADE B 502
ChainResidue
BILE15
BTYR168
BLYS208
BARG7
BTYR14

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11171970, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1HQC, ECO:0000312|PDB:1IXS
ChainResidueDetails
ATYR14
BTYR14

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11171970, ECO:0000312|PDB:1HQC, ECO:0000312|PDB:1IXS
ChainResidueDetails
AILE15
BILE15

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1IXR
ChainResidueDetails
AGLY48
BGLY48

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1IXR, ECO:0000312|PDB:1IXS
ChainResidueDetails
ALYS51
ATHR53
BLYS51
BTHR53

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016
ChainResidueDetails
ATHR52
AARG297
AARG302
BTHR52
BARG297
BARG302

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:12408833
ChainResidueDetails
AASP97
ATHR146
BASP97
BTHR146

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:11171970, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1HQC, ECO:0000312|PDB:1IXS
ChainResidueDetails
ATYR168
BTYR168

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000305|PubMed:12408833
ChainResidueDetails
AARG205
BARG205

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10464259, 11171970
ChainResidueDetails
ATHR146
AARG205

site_idCSA2
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10464259, 11171970
ChainResidueDetails
BTHR146
BARG205

site_idMCSA1
Number of Residues5
DetailsM-CSA 780
ChainResidueDetails
ALYS51
ATHR52
AASP97
ATHR146electrostatic stabiliser
AARG205electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 780
ChainResidueDetails
BLYS51
BTHR52
BASP97
BTHR146electrostatic stabiliser
BARG205electrostatic stabiliser

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon