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

1XJF

Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005524molecular_functionATP binding
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0031419molecular_functioncobalamin binding
B0000166molecular_functionnucleotide binding
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005524molecular_functionATP binding
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0031419molecular_functioncobalamin binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 1003
ChainResidue
BDTP1001

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 1004
ChainResidue
ADTP1002

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE DTP B 1001
ChainResidue
BARG171
BVAL177
BALA178
BGLY179
BTHR180
BLYS183
BALA184
BSER185
BPHE190
BMG1003
BHOH1005
ALYS158
AVAL200
ALYS202
BASP141
BSER142
BILE143
BILE146

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE DTP A 1002
ChainResidue
AASP141
ASER142
AILE143
AILE146
AARG171
AVAL177
AALA178
AGLY179
ATHR180
ALYS183
AALA184
ASER185
APHE190
AMG1004
AHOH1026
BLYS158
BVAL200
BVAL201
BLYS202

225158

PDB entries from 2024-09-18

PDB statisticsPDBj update infoContact PDBjnumon