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

1VCO

Crystal Structure of T.th. HB8 CTP synthetase complex with Glutamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003883molecular_functionCTP synthase activity
A0004359molecular_functionglutaminase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006241biological_processCTP biosynthetic process
A0006541biological_processglutamine metabolic process
A0016874molecular_functionligase activity
A0019856biological_processpyrimidine nucleobase biosynthetic process
A0042802molecular_functionidentical protein binding
A0044210biological_process'de novo' CTP biosynthetic process
A0046872molecular_functionmetal ion binding
A0097268cellular_componentcytoophidium
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLN A 610
ChainResidue
ATYR64
AARG472
ATYR473
AHOH753
AGLY363
AGLY364
APHE365
ACYS391
ALEU392
AGLN395
AGLU415
AHIS471

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile; for glutamine hydrolysis => ECO:0000255|HAMAP-Rule:MF_01227, ECO:0000305|PubMed:15296735
ChainResidueDetails
ACYS391

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01227, ECO:0000305|PubMed:15296735
ChainResidueDetails
AHIS522
AGLU524

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01227
ChainResidueDetails
ASER23
ASER24
AASP81
AGLU151
AASP158
ALYS198
ALYS234
AVAL252

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15296735, ECO:0007744|PDB:1VCO
ChainResidueDetails
ATYR64
AGLY364
ALEU392
AGLU415
AARG472

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon