Structure of PDB 2a5h Chain D Binding Site BS03

Receptor Information
>2a5h Chain D (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 IDSAM
InChIInChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/t7-,8+,10+,11+,14+,27-/m0/s1
InChIKeyMEFKEPWMEQBLKI-FCKMPRQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[S@@+](CC[C@H](N)C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S+](CCC(C(=O)[O-])N)CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.341C[S+](CC[CH](N)C([O-])=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S@@+](CC[C@@H](C(=O)[O-])N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
ACDLabs 10.04[O-]C(=O)C(N)CC[S+](C)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H22 N6 O5 S
NameS-ADENOSYLMETHIONINE
ChEMBLCHEMBL1235831
DrugBank
ZINC
PDB chain2a5h Chain D Residue 417 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2a5h The X-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		H131 T133 R134 S169 G171 H230 Q258 V260 Y290 C292 D293
Binding residue
(residue number reindexed from 1)		H129 T131 R132 S167 G169 H228 Q256 V258 Y288 C290 D291
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)

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