Structure of PDB 2a5h Chain C

Receptor sequence
>2a5hC (length=409) Species: 1550 (Clostridium subterminale) [Search protein sequence]
NRRYELFKDVSDADWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCV
KSLRMAITPYYLSLIDPNDPNDPVRKQAIPTALELNKAAADLEDPLHEDT
DSPVPGLTHRYPDRVLLLITDMCSMYCRHCTRRRFAGQSDDSMPMERIDK
AIDYIRNTPQVRDVLLSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSR
TPVVLPQRITPELVNMLKKYHPVWLNTHFNHPNEITEESTRACQLLADAG
VPLGNQSVLLRGVNDCVHVMKELVNKLVKIRVRPYYIYQCDLSLGLEHFR
TPVSKGIEIIEGLRGHTSGYCVPTFVVDAPGGGGKTPVMPNYVISQSHDK
VILRNFEGVITTYSEPINYTPGCNCDVCTGKKKVHKVGVAGLLNGEGMAL
EPVGLERNK
3D structure
PDB2a5h The X-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale.
ChainC
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R112 Y113 R116 C125 C129 C132 R134 D293 D330 K337
Catalytic site (residue number reindexed from 1) R110 Y111 R114 C123 C127 C130 R132 D291 D328 K335
Enzyme Commision number 5.4.3.2: lysine 2,3-aminomutase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
GO:0050066 L-lysine 2,3-aminomutase activity
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0019475 L-lysine catabolic process to acetate

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Molecular Function
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Biological Process
External links
PDB RCSB:2a5h, PDBe:2a5h, PDBj:2a5h
PDBsum2a5h
PubMed16166264
UniProtQ9XBQ8|KAMA_CLOSU L-lysine 2,3-aminomutase (Gene Name=kamA)

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