Structure of PDB 3msu Chain B

Receptor sequence
>3msuB (length=426) Species: 263 (Francisella tularensis) [Search protein sequence]
NAMEVMLMSKYATLKYADKNIEIELPVYSPSLGNDCIDVSSLVKHGIFTY
DPGFMSTAACESKITYIDGGKGVLLHRGYPIEEWTQKSNYRTLCYALIYG
ELPTDEQVKSFRQEIINKMPVCEHVKAAIAAMPQHTHPMSSLIAGVNVLA
AEHIHNGQKESQDEVAKNIVAKIATIAAMAYRHNHGKKFLEPKMEYGYAE
NFLYMMFADDESYKPDELHIKAMDTIFMLHADHEQNASTSTVRLSGSTGN
SPYAAIIAGITALWGPAHGGANEAVLKMLSEIGSTENIDKYIAKAKDKDD
PFRLMGFGHRVYKNTDPRATAMKKNCEEILAKLGHSDNPLLTVAKKLEEI
ALQDEFFIERKLFSNVDFYSGIILKAMGIPEDMFTAIFALARTSGWISQW
IEMVNDPAQKIGRPRQLYTGATNRNF
3D structure
PDB3msu Crystal Structure of Citrate Synthase from Francisella tularensis
ChainB
Resolution1.843 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S236 H266 H307 R316 D365
Catalytic site (residue number reindexed from 1) S238 H268 H309 R318 D367
Enzyme Commision number 2.3.3.16: citrate synthase (unknown stereospecificity).
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 OAA B Y88 R89 C92 R110 Y196 Y90 R91 C94 R112 Y198
Gene Ontology
Molecular Function
GO:0004108 citrate (Si)-synthase activity
GO:0016746 acyltransferase activity
GO:0036440 citrate synthase activity
GO:0046872 metal ion binding
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0006099 tricarboxylic acid cycle
Cellular Component
GO:0005737 cytoplasm

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Biological Process
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Cellular Component
External links
PDB RCSB:3msu, PDBe:3msu, PDBj:3msu
PDBsum3msu
PubMed
UniProtQ5NIJ6

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