Structure of PDB 1mly Chain B Binding Site BS02

Receptor Information
>1mly Chain B (length=428) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMS
SWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTP
QPLECVFLADSGSVAVEVAMKMALQYWQAKGEARQRFLTFRNGYHGDTFG
AMSVCDPDNSMHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAA
HRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGILLIADEIATG
FGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGE
AGCFMHGPTFMGNPLACAAANASLAILESGDWQQQVADIEVQLREQLAPA
RDAEMVADVRVLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLM
PPYIILPQQLQRLTAAVNRAVQDETFFC
Ligand information
Ligand IDACZ
InChIInChI=1S/C10H16N2O2/c11-8-4-1-7(2-5-8)3-6-9(12)10(13)14/h1-2,4-5,7-9H,3,6,11-12H2,(H,13,14)/t7-,8?,9-/m0/s1
InChIKeyLAJWZJCOWPUSOA-SMOXQLQSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1=CC(C=CC1CCC(C(=O)O)N)N
CACTVS 3.341N[C@@H](CC[C@@H]1C=C[C@@H](N)C=C1)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCC1C=CC(N)C=C1
OpenEye OEToolkits 1.5.0C1=CC(C=CC1CC[C@@H](C(=O)O)N)N
CACTVS 3.341N[CH](CC[CH]1C=C[CH](N)C=C1)C(O)=O
FormulaC10 H16 N2 O2
NameCIS-AMICLENOMYCIN;
2-AMINO-4-(4-AMINO-CYCLOHEXA-2,5-DIENYL)-BUTYRIC ACID
ChEMBL
DrugBankDB02725
ZINC
PDB chain1mly Chain B Residue 831 [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]
PDB1mly Structural basis for the inhibition of the biosynthesis of biotin by the antibiotic amiclenomycin
Resolution1.81 Å
Binding residue
(original residue number in PDB)		Y144 F393
Binding residue
(residue number reindexed from 1)		Y144 F393
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y17 Y144 E211 D245 A248 K274 Y398
Catalytic site (residue number reindexed from 1) Y17 Y144 E211 D245 A248 K274 Y398
Enzyme Commision number 2.6.1.62: adenosylmethionine--8-amino-7-oxononanoate transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004015 adenosylmethionine-8-amino-7-oxononanoate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0009102 biotin biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1mly, PDBe:1mly, PDBj:1mly
PDBsum1mly
PubMed12218056
UniProtP12995|BIOA_ECOLI Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (Gene Name=bioA)

[Back to BioLiP]