Structure of PDB 3doc Chain A

Receptor sequence
>3docA (length=335) Species: 359391 (Brucella abortus 2308) [Search protein sequence]
MAVRVAINGFGRIGRNILRAIVESGRTDIQVVAINDLGPVETNAHLLRYD
SVHGRFPKEVEVAGDTIDVGYGPIKVHAVRNPAELPWKEENVDIALECTG
IFTSRDKAALHLEAGAKRVIVSAPADGADLTVVYGVNNDKLTKDHLVISN
ASCTTNCLAPVAQVLNDTIGIEKGFMTTIHSYTGDQPTLDTMHKDLYRAR
AAALSMIPTSTGAAKAVGLVLPELKGKLDGVAIRVPTPNVSVVDLTFIAK
RETTVEEVNNAIREAANGRLKGILGYTDEKLVSHDFNHDSHSSVFHTDQT
KVMDGTMVRILSWYDNEWGFSSRMSDTAVALGKLI
3D structure
PDB3doc Crystal Structure of TrkA glyceraldehyde-3-phosphate dehydrogenase from Brucella melitensis
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C153 H180
Catalytic site (residue number reindexed from 1) C153 H180
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 NAD A G9 F10 G11 R12 I13 D36 S122 C153 N316 E317 F320 G9 F10 G11 R12 I13 D36 S122 C153 N316 E317 F320
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:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0006006 glucose metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3doc, PDBe:3doc, PDBj:3doc
PDBsum3doc
PubMed
UniProtQ2YRE0

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