Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3L0D

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0006006biological_processglucose metabolic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0006006biological_processglucose metabolic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
AHIS180
ACYS153

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
BHIS180
BCYS153

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon