Structure of PDB 1dty Chain B

Receptor sequence
>1dtyB (length=429) Species: 562 (Escherichia coli) [Search protein sequence]
MTTDDLAFDERHIWHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMS
SWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGEITHAPAIELCRKLVAMTP
QPLECVFLADSGSVAVEVAMKMALQYWDAKGEARDRFLTFRNGYHGDTFG
AMSVCDPDNSMHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAA
HRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGILLIADEIATG
FGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISDGE
AGCFMHGPTFMGNPLACAAANASLAILESGDWQQQVADIEVQLREQLAPA
RDAEMVADVRVLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLM
PPYIILPQQLQRLTAAVNRAVQDETFFCQ
3D structure
PDB1dty Crystal structure of adenosylmethionine-8-amino-7-oxonanoate aminotransferase with pyridoxal phosphate cofactor
ChainB
Resolution2.14 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 PLP B P308 T309 P308 T309
BS02 PLP B G112 S113 Y144 H145 D245 I247 A248 K274 G112 S113 Y144 H145 D245 I247 A248 K274
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dty, PDBe:1dty, PDBj:1dty
PDBsum1dty
PubMed
UniProtP12995|BIOA_ECOLI Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (Gene Name=bioA)

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