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

1VCN

Crystal Structure of T.th. HB8 CTP synthetase complex with Sulfate anion

Functional Information from GO Data
ChainGOidnamespacecontents
A0003883molecular_functionCTP synthase activity
A0004359molecular_functionglutaminase activity
A0005524molecular_functionATP binding
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006241biological_processCTP biosynthetic process
A0006541biological_processglutamine metabolic process
A0016874molecular_functionligase activity
A0044210biological_process'de novo' CTP biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 610
ChainResidue
ALYS27
ALYS49
AGLU151
AGLY153
AGLY154
AHOH644
AHOH873

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 620
ChainResidue
AGLY26
ALYS27
AGLY28
AHOH637
AHOH638
AHOH648
ASER24
ALEU25

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 630
ChainResidue
ALYS198
ATHR199
ALYS200
ALYS234
AHOH662
AHOH719

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
ACYS391
AHIS522
AGLU524

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bxr
ChainResidueDetails
ACYS391
AHIS522

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon