Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5HRL

The crystal structure of AsfvPolX: 1nt-gap(P) DNA2: dGTP ternary 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
A0016779molecular_functionnucleotidyltransferase activity
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
B0016779molecular_functionnucleotidyltransferase activity
B0044423cellular_componentvirion component
B0046872molecular_functionmetal ion binding
B0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue DGT A 201
ChainResidue
AGLY38
AGLY118
AVAL120
ALEU123
AMN202
AMN203
AGOL204
AHOH301
AHOH304
AHOH310
AHOH315
ASER39
CDG9
CHOH101
DDA9
AARG42
AASN48
AASP49
AASP51
AHIS115
APHE116
ATHR117

site_idAC2
Number of Residues5
Detailsbinding site for residue MN A 202
ChainResidue
AASP49
AASP51
ADGT201
AMN203
AHOH301

site_idAC3
Number of Residues5
Detailsbinding site for residue MN A 203
ChainResidue
AASP49
AASP51
AASP100
ADGT201
AMN202

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 204
ChainResidue
AGLU44
AMET46
ADGT201
BGLY-1

site_idAC5
Number of Residues18
Detailsbinding site for residue DGT B 201
ChainResidue
BGLY38
BSER39
BARG42
BASN48
BASP49
BASP51
BHIS115
BPHE116
BTHR117
BGLY118
BVAL120
BLEU123
BMN202
BMN203
BHOH305
FDG9
FHOH102
GDA9

site_idAC6
Number of Residues5
Detailsbinding site for residue MN B 202
ChainResidue
BASP49
BASP51
BDGT201
BMN203
BHOH305

site_idAC7
Number of Residues5
Detailsbinding site for residue MN B 203
ChainResidue
BASP49
BASP51
BASP100
BDGT201
BMN202

Functional Information from PROSITE/UniProt
site_idPS00522
Number of Residues20
DetailsDNA_POLYMERASE_X DNA polymerase family X signature. GSLrREekmLnDVDLLIivP
ChainResidueDetails
AGLY38-PRO57

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11685239, ECO:0000305|PubMed:28245220
ChainResidueDetails
AASP49
AASP51
AASP100
BASP49
BASP51
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

PDB statisticsPDBj update infoContact PDBjnumon