Structure of PDB 1qj5 Chain B

Receptor sequence
>1qj5B (length=429) Species: 469008 (Escherichia coli BL21(DE3)) [Search protein sequence]
MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMS
SWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTP
QPLECVFLADSGSVAVEVAMKMALQYWQAKGEARQRFLTFRNGYHGDTFG
AMSVCDPDNSMHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAA
HRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGILLIADEIATG
FGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGE
AGCFMHGPTFMGNPLACAAANASLAILESGDWQQQVADIEVQLREQLAPA
RDAEMVADVRVLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLM
PPYIILPQQLQRLTAAVNRAVQDETFFCQ
3D structure
PDB1qj5 Crystal Structure of Diaminopelargonic Acid Synthase; Evolutionary Relationships between Pyridoxal-5'-Phosphate Dependent Enzymes
ChainB
Resolution1.8 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 G112 S113 Y144 H145 E211 D245 I247 K274 G112 S113 Y144 H145 E211 D245 I247 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:1qj5, PDBe:1qj5, PDBj:1qj5
PDBsum1qj5
PubMed10452893
UniProtP12995|BIOA_ECOLI Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (Gene Name=bioA)

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