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

3O5T

Structure of DraG-GlnZ complex with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046872molecular_functionmetal ion binding
A0047407molecular_functionADP-ribosyl-[dinitrogen reductase] hydrolase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006808biological_processregulation of nitrogen utilization
B0030234molecular_functionenzyme regulator activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 298
ChainResidue
AGLU28
AASP243
AASP245
ATHR246
AHOH565
AHOH586

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 299
ChainResidue
AASP245
AHOH345
ATHR59
AASP60
AASP61

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ADP B 113
ChainResidue
AHOH482
BILE7
BGLY27
BLEU28
BTHR29
BGLY35
BPHE36
BGLY37
BARG38
BGLN39
BLYS58
BGLU62
BVAL63
BALA64
BILE86
BGLY87
BGLY89
BLYS90
BARG101
BARG103
BHOH118
BHOH143
BHOH236
BHOH256

Functional Information from PROSITE/UniProt
site_idPS00496
Number of Residues6
DetailsPII_GLNB_UMP P-II protein uridylation site. YRGAEY
ChainResidueDetails
BTYR46-TYR51

site_idPS00638
Number of Residues14
DetailsPII_GLNB_CTER P-II protein C-terminal region signature. TgriGDGKIFVldI
ChainResidueDetails
BTHR83-ILE96

223790

PDB entries from 2024-08-14

PDB statisticsPDBj update infoContact PDBjnumon