Structure of PDB 5e9x Chain A

Receptor sequence
>5e9xA (length=715) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
TDRVSVGNLRIARVLYDFVNNEALPGTDIDPDSFWAGVDKVVADLTPQNQ
ALLNARDELQAQIDKWHRRRPIDMDAYRQFLTEIGYLLPEPDDFTITTSG
VDAEITTTAGPQLVVPVLNARFALNAANARWGSLYDALYGTDVIPETDGA
EKGPTYNKVRGDKVIAYARKFLDDSVPLSSGSFGDATGFTVQDGQLVVAL
PDKSTGLANPGQFAGYTGAAESPTSVLLINHGLHIEILIDPESQVGTTDR
AGVKDVILESAITTIMDFEDSVAAVDAADKVLGYRNWLGLNKGDLAAAVR
VLNRDRNYTAPGGGQFTLPGRSLMFVRNVGHLMTNDAIVDTDGSEVFEGI
MDALFTGLIAIHGLKASDVNGPLINSRTGSIYIVKPKMHGPAEVAFTCEL
FSRVEDVLGLPQNTMKIGIMDEERRTTVNLKACIKAAADRVVFINTGFLD
RTGDEIHTSMEAGPMVRKGTMKSQPWILAYEDHNVDAGLAAGFSGRAQVG
KGMWTMTELMADMVETKIAQPRAGASTAWVPSPTAATLHALHYHQVDVAA
VQQGLAGKRRATIEQLLTIPLAKELAWAPDEIREEVDNNCQSILGYVVRW
VDQGVGASKVPDIHDVALMEDRATLRISSQLLANWLRHGVITSADVRASL
ERMAPLVDRQNAGDVAYRPMAPNFDDSIAFLAAQELILSGAQQPNGYTEP
ILHRRRREFKARAAE
3D structure
PDB5e9x Mycobacterium tuberculosis Malate Synthase Structures with Fragments Reveal a Portal for Substrate/Product Exchange.
ChainA
Resolution1.943 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D271 E273 R339 E434 D462 D633
Catalytic site (residue number reindexed from 1) D267 E269 R327 E422 D450 D621
Enzyme Commision number 2.3.3.9: malate synthase.
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 MG A E434 D462 E422 D450
BS02 5LA A V118 S275 M515 M631 E632 D633 V114 S271 M503 M619 E620 D621
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0001968 fibronectin binding
GO:0003824 catalytic activity
GO:0004474 malate synthase activity
GO:0005515 protein binding
GO:0005518 collagen binding
GO:0016740 transferase activity
GO:0042803 protein homodimerization activity
GO:0043236 laminin binding
GO:0046810 host cell extracellular matrix binding
GO:0046872 metal ion binding
GO:0120225 coenzyme A binding
Biological Process
GO:0006097 glyoxylate cycle
GO:0006099 tricarboxylic acid cycle
GO:0009436 glyoxylate catabolic process
GO:0015936 coenzyme A metabolic process
GO:0044406 adhesion of symbiont to host
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall
GO:0009986 cell surface
GO:0042603 capsule

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5e9x, PDBe:5e9x, PDBj:5e9x
PDBsum5e9x
PubMed27738104
UniProtP9WK17|MASZ_MYCTU Malate synthase G (Gene Name=glcB)

[Back to BioLiP]