Structure of PDB 1mly Chain A

Receptor sequence

>1mlyA (length=427) Species: 562 (Escherichia coli)

MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMS
SWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTP
QPLECVFLADSGSVAVEVAMKMALQYWQAKGEARQRFLTFRNGYHGDTFG
AMSVCDPDNSMHSLWKGYLPENLFAPAPQSRMGEWDERDMVGFARLMAAH
RHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGILLIADEIATGF
GRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGEA
GCFMHGPTFMGNPLACAAANASLAILESGDWQQQVADIEVQLREQLAPAR
DAEMVADVRVLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLMP
PYIILPQQLQRLTAAVNRAVQDETFFC

3D structure

• PDB: 1mly Structural basis for the inhibition of the biosynthesis of biotin by the antibiotic amiclenomycin
• Chain: A
• Resolution: 1.81 Å

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 E210 D244 A247 K273 Y397
• Enzyme Commision number: 2.6.1.62: adenosylmethionine--8-amino-7-oxononanoate transaminase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ACZ	A	W52 W53 K274 R391 F393	W52 W53 K273 R390 F392
BS02	PLP	A	G112 S113 Y144 H145 D245 I247 K274	G112 S113 Y144 H145 D244 I246 K273
BS03	PLP	A	P308 T309	P307 T308

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

External links

• PDB: RCSB:1mly, PDBe:1mly, PDBj:1mly
• PDBsum: 1mly
• PubMed: 12218056
• UniProt: P12995|BIOA_ECOLI Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (Gene Name=bioA)