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

5L9N

Structure of uridylylated GlnB from Escherichia coli bound to ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006808biological_processregulation of nitrogen utilization
A0008047molecular_functionenzyme activator activity
A0030234molecular_functionenzyme regulator activity
A0036094molecular_functionsmall molecule binding
A0042304biological_processregulation of fatty acid biosynthetic process
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ATP A 201
ChainResidue
AILE7
ALYS85
AILE86
AGLY87
AASP88
AGLY89
ALYS90
AARG101
AILE102
AARG103
AGLY27
AMET28
ATHR29
AGLY35
ALYS58
AGLU62
AILE63
AVAL64

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 202
ChainResidue
APHE11
APHE11
AASP14
AASP14
AASP15
AASP15

Functional Information from PROSITE/UniProt
site_idPS00496
Number of Residues6
DetailsPII_GLNB_UMP P-II protein uridylation site. YRGAEY
ChainResidueDetails
ATYR46-TYR51

site_idPS00638
Number of Residues14
DetailsPII_GLNB_CTER P-II protein C-terminal region signature. TgkiGDGKIFVfdV
ChainResidueDetails
ATHR83-VAL96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675, ECO:0000269|PubMed:2885322
ChainResidueDetails
ATYR51

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon