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3DOC

Crystal Structure of TrkA glyceraldehyde-3-phosphate dehydrogenase from Brucella melitensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0048046cellular_componentapoplast
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0048046cellular_componentapoplast
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
C0000166molecular_functionnucleotide binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005829cellular_componentcytosol
C0006006biological_processglucose metabolic process
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0048046cellular_componentapoplast
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D0005829cellular_componentcytosol
D0006006biological_processglucose metabolic process
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0048046cellular_componentapoplast
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE NAD A 901
ChainResidue
AGLY9
AASN316
AGLU317
APHE320
APHE10
AGLY11
AARG12
AILE13
AASP36
ASER122
AALA123
ACYS153

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAD B 901
ChainResidue
BGLY9
BGLY11
BARG12
BILE13
BASN35
BASP36
BARG80
BCYS98
BTHR99
BGLY100
BSER122
BALA123
BCYS153
BASN316

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAD D 901
ChainResidue
DGLY9
DGLY11
DARG12
DILE13
DASN35
DASP36
DLEU37
DARG80
DCYS98
DTHR99
DGLY100
DSER122
DALA123
DASN316

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAD C 901
ChainResidue
CGLY9
CGLY11
CARG12
CILE13
CASN35
CASP36
CLEU37
CARG80
CCYS98
CTHR99
CGLY100
CSER122
CALA123
CCYS153
CASN316

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA151-LEU158

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PDB entries from 2024-06-12

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