Structure of PDB 2a5h Chain B Binding Site BS05

Receptor Information
>2a5h Chain B (length=410) Species: 1550 (Clostridium subterminale) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NRRYELFKDVSDADWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCV
KSLRMAITPYYLSLIDPNDPNDPVRKQAIPTALELNKAAADLEDPLHEDT
DSPVPGLTHRYPDRVLLLITDMCSMYCRHCTRRRFAGQSDDSMPMERIDK
AIDYIRNTPQVRDVLLSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSR
TPVVLPQRITPELVNMLKKYHPVWLNTHFNHPNEITEESTRACQLLADAG
VPLGNQSVLLRGVNDCVHVMKELVNKLVKIRVRPYYIYQCDLSLGLEHFR
TPVSKGIEIIEGLRGHTSGYCVPTFVVDAPGGGGKTPVMPNYVISQSHDK
VILRNFEGVITTYSEPINYTPGCNCDVCTGKKKVHKVGVAGLLNGEGMAL
EPVGLERNKR
Ligand information
Ligand IDSF4
InChIInChI=1S/4Fe.4S
InChIKeyLJBDFODJNLIPKO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7[S]12[Fe]3[S]4[Fe]1[S]5[Fe]2[S]3[Fe]45
CACTVS 3.385S1[Fe]S[Fe]1.S2[Fe]S[Fe]2
FormulaFe4 S4
NameIRON/SULFUR CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain2a5h Chain B Residue 418 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2a5h The X-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		C125 C129 C132 G171 R202 H230
Binding residue
(residue number reindexed from 1)		C123 C127 C130 G169 R200 H228
Annotation score1
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

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

[Back to BioLiP]