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3L0D

Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Bartonella henselae with bound NAD

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
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD A 336
ChainResidue
AGLY9
AGLY100
AILE101
ASER122
AALA123
ACYS153
AASN316
AGLU317
APHE320
AHOH405
AHOH409
APHE10
AHOH410
AGLY11
AARG12
AILE13
AASN35
AASP36
ACYS98
ATHR99

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAD B 336
ChainResidue
ATHR191
AMET192
BGLY11
BARG12
BILE13
BASP36
BARG80
BCYS98
BTHR99
BGLY100
BILE101
BSER122
BALA123
BCYS153
BASN316

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

221051

PDB entries from 2024-06-12

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