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

1XJM

Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dTTP 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 A 1005
ChainResidue
ATTP1001

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 1006
ChainResidue
BTTP1002
BHOH1112

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE TTP A 1001
ChainResidue
AGLY179
ATHR180
AALA184
ASER185
APHE190
AMG1005
AHOH1009
BLYS158
BVAL200
BVAL201
AASP141
ASER142
AILE143
AARG171
AVAL177
AALA178

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TTP B 1002
ChainResidue
ALYS158
AVAL201
BASP141
BSER142
BILE143
BARG171
BVAL177
BALA178
BGLY179
BALA184
BSER185
BPHE190
BMG1006
BHOH1036

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TTP B 1003
ChainResidue
BARG26
BSER91
BALA133
BGLU324
BLEU335
BALA489
BPRO490
BTHR491
BGLY492
BSER493
BILE494
BHOH1037
BHOH1074

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TTP A 1004
ChainResidue
AARG26
ASER91
AALA133
AASN320
AGLU324
ALEU335
APRO490
ATHR491
AGLY492
ASER493
AILE494
AHOH1056
AHOH1106
AHOH1107

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon