Structure of PDB 1kcz Chain B

Receptor sequence
>1kczB (length=413) Species: 1553 (Clostridium tetanomorphum) [Search protein sequence]
MKIVDVLCTPGLTGFYFDDQRAIKKGAGHDGFTYTGSTVTEGFTQVRQKG
ESISVLLVLEDGQVAHGDCAAVQYSGAGGRDPLFLAKDFIPVIEKEIAPK
LIGREITNFKPMAEEFDKMTVNGNRLHTAIRYGITQAILDAVAKTRKVTM
AEVIRDEYNPGAEINAVPVFAQSGDDRYDNVDKMIIKEADVLPHALINNV
EEKLGLKGEKLLEYVKWLRDRIIKLRVREDYAPIFHIDVYGTIGAAFDVD
IKAMADYIQTLAEAAKPFHLRIEGPMDVEDRQKQMEAMRDLRAELDGRGV
DAELVADEWCNTVEDVKFFTDNKAGHMVQIKTPDLGGVNNIADAIMYCKA
NGMGAYCGGTCNETNRSAEVTTNIGMACGARQVLAKPGMGVDEGMMIVKN
EMNRVLALVGRRK
3D structure
PDB1kcz The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q172 H194 D238 E273 D307 Q329 K331
Catalytic site (residue number reindexed from 1) Q172 H194 D238 E273 D307 Q329 K331
Enzyme Commision number 4.3.1.2: methylaspartate ammonia-lyase.
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 B D238 E273 D307 D238 E273 D307
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0031419 cobalamin binding
GO:0046872 metal ion binding
GO:0050096 methylaspartate ammonia-lyase activity
Biological Process
GO:0019553 glutamate catabolic process via L-citramalate

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Molecular Function
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Biological Process
External links
PDB RCSB:1kcz, PDBe:1kcz, PDBj:1kcz
PDBsum1kcz
PubMed11748244
UniProtQ05514|MAAL_CLOTT Methylaspartate ammonia-lyase

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