Structure of PDB 3zdf Chain B

Receptor sequence
>3zdfB (length=338) Species: 146786 (Thermosynechococcus vestitus) [Search protein sequence]
SMVRVAINGFGRIGRNFMRCWLQRKANSKLEIVGINDTSDPRTNAHLLKY
DSMLGIFQDAEITADDDCIYAGGHAVKCVSDRNPENLPWSAWGIDLVIEA
TGVFTSREGASKHLSAGAKKVLITAPGKGNIPTYVVGVNHHTYDPSEDIV
SNASCTTNCLAPIVKVLHEAFGIQQGMMTTTHSYTGDQRLLDASHRDLRR
ARAAAMNIVPTSTGAAKAVGLVIPELQGKLNGIALRVPTPNVSVVDFVAQ
VEKPTIAEQVNQVIKEASETTMKGIIHYSELELVSSDYRGHNASSILDAS
LTMVLGGNLVKVVAWYDNEWGYSQRVLDLAEHMAAHWA
3D structure
PDB3zdf Structure of Gapdh
ChainB
Resolution2.34 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C154 H181
Catalytic site (residue number reindexed from 1) C155 H182
Enzyme Commision number 1.2.1.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide B R81 V102 T155 H181 T184 D186 R188 S193 H194 R195 R199 T212 G213 R235 R82 V103 T156 H182 T185 D187 R189 S194 H195 R196 R200 T213 G214 R236
BS02 NAD B G10 R11 I12 D36 T37 R81 T100 G101 T123 C154 N317 Y321 G11 R12 I13 D37 T38 R82 T101 G102 T124 C155 N318 Y322
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0006006 glucose metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3zdf, PDBe:3zdf, PDBj:3zdf
PDBsum3zdf
PubMed
UniProtQ8DIW5

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