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2GGQ

complex of hypothetical glucose-1-phosphate thymidylyltransferase from sulfolobus tokodaii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003977molecular_functionUDP-N-acetylglucosamine diphosphorylase activity
A0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0008879molecular_functionglucose-1-phosphate thymidylyltransferase activity
A0009058biological_processbiosynthetic process
A0016746molecular_functionacyltransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0019134molecular_functionglucosamine-1-phosphate N-acetyltransferase activity
A0052630molecular_functionUDP-N-acetylgalactosamine diphosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 501
ChainResidue
ATYR311

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 502
ChainResidue
APHE334

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TTP A 500
ChainResidue
ALYS23
AGLN73
AGLY79
AALA83
AARG179
AGLU181
ALYS344
AHOH622
ALEU6
AALA8
AGLY9
ASER10
AGLY11
AGLU12
AARG13

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:30291121, ECO:0000269|Ref.6
ChainResidueDetails
AALA8
AGLN73
AGLY79

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:30291121, ECO:0007744|PDB:5Z0A
ChainResidueDetails
ATHR80
ATYR97
AGLY131
AGLU146
AASN157

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
AARG13

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1lxa
ChainResidueDetails
AGLY261

226707

PDB entries from 2024-10-30

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