Structure of PDB 2a5h Chain C Binding Site BS05

Receptor Information

>2a5h Chain C (length=409) Species: 1550 (Clostridium subterminale)

NRRYELFKDVSDADWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCV
KSLRMAITPYYLSLIDPNDPNDPVRKQAIPTALELNKAAADLEDPLHEDT
DSPVPGLTHRYPDRVLLLITDMCSMYCRHCTRRRFAGQSDDSMPMERIDK
AIDYIRNTPQVRDVLLSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSR
TPVVLPQRITPELVNMLKKYHPVWLNTHFNHPNEITEESTRACQLLADAG
VPLGNQSVLLRGVNDCVHVMKELVNKLVKIRVRPYYIYQCDLSLGLEHFR
TPVSKGIEIIEGLRGHTSGYCVPTFVVDAPGGGGKTPVMPNYVISQSHDK
VILRNFEGVITTYSEPINYTPGCNCDVCTGKKKVHKVGVAGLLNGEGMAL
EPVGLERNK

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 2a5h Chain D Residue 421

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2a5h The X-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale.
• Resolution: 2.1 Å
• Binding residue (original residue number in PDB): C375 C377 C380
• Binding residue (residue number reindexed from 1): C373 C375 C378
• Annotation score: 1

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.

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

External links

• PDB: RCSB:2a5h, PDBe:2a5h, PDBj:2a5h
• PDBsum: 2a5h
• PubMed: 16166264
• UniProt: Q9XBQ8|KAMA_CLOSU L-lysine 2,3-aminomutase (Gene Name=kamA)