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2CB0

Crystal structure of glucosamine 6-phosphate deaminase from Pyrococcus furiosus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004360molecular_functionglutamine-fructose-6-phosphate transaminase (isomerizing) activity
A0006002biological_processfructose 6-phosphate metabolic process
A0006047biological_processUDP-N-acetylglucosamine metabolic process
A0006487biological_processprotein N-linked glycosylation
A0008483molecular_functiontransaminase activity
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
B0004360molecular_functionglutamine-fructose-6-phosphate transaminase (isomerizing) activity
B0006002biological_processfructose 6-phosphate metabolic process
B0006047biological_processUDP-N-acetylglucosamine metabolic process
B0006487biological_processprotein N-linked glycosylation
B0008483molecular_functiontransaminase activity
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1321
ChainResidue
AILE102
AASN103
ATHR104
ALYS106
AASP121
AHOH2172
BGLU91
BARG324

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1jxa
ChainResidueDetails
AHIS227
BGLU204
BLYS208
BLYS321

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1jxa
ChainResidueDetails
AGLU204
ALYS208
BHIS227

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PDB entries from 2024-07-31

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