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5HRG

The crystal structure of AsfvPolX(D51N mutant):DNA4 binary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0006259biological_processDNA metabolic process
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0009059biological_processmacromolecule biosynthetic process
A0044423cellular_componentvirion component
A0046872molecular_functionmetal ion binding
A0071897biological_processDNA biosynthetic process
B0003677molecular_functionDNA binding
B0003887molecular_functionDNA-directed DNA polymerase activity
B0006259biological_processDNA metabolic process
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0006303biological_processdouble-strand break repair via nonhomologous end joining
B0009059biological_processmacromolecule biosynthetic process
B0044423cellular_componentvirion component
B0046872molecular_functionmetal ion binding
B0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 201
ChainResidue
AASP49
AASN51
AASP100
CDG7
CDC8
CHOH104

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 202
ChainResidue
AARG168
AHOH306
BLYS9
AARG125
APHE165
ATHR166

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 203
ChainResidue
AASN12
AHIS13
AARG17

site_idAC4
Number of Residues5
Detailsbinding site for residue MN B 201
ChainResidue
BASP49
BASN51
BASP100
DDG7
DDC8

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 B 202
ChainResidue
BARG125
BPHE165
BTHR166
BARG168

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 B 203
ChainResidue
BASN12
BHIS13
BARG17

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 B 204
ChainResidue
BTYR22
BLYS60
BLYS63
BHIS64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11685239, ECO:0000305|PubMed:28245220
ChainResidueDetails
AASP49
AASN51
AASP100
BASP49
BASN51
BASP100

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Stabilizes dGTP in a syn confromation to overcome the Watson-Crick base pairing constraint => ECO:0000269|PubMed:24617852
ChainResidueDetails
AHIS115
BHIS115

220113

PDB entries from 2024-05-22

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