Structure of PDB 1qj3 Chain A

Receptor sequence

>1qj3A (length=416) Species: 469008 (Escherichia coli BL21(DE3))

MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMS
SWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTP
QPLECVFLADSGSVAVEVAMKMALQYWQAKGEARQRFLTFRNGYHGDTFG
AMSVCDPDNLPENLFAPAPQSRMGEWDERDMVGFARLMAAHRHEIAAVII
EPIVQGAGGMRMYHPEWLKRIRKICDREGILLIADEIATGFGRTGKLFAC
EHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGGCFMHGPTFMG
NPLACAAANASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVRVL
GAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLMPPYIILPQQLQR
LTAAVNRAVQDETFFC

3D structure

• PDB: 1qj3 Crystal Structure of Diaminopelargonic Acid Synthase; Evolutionary Relationships between Pyridoxal-5'-Phosphate Dependent Enzymes
• Chain: A
• Resolution: 2.7 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 E201 D235 A238 K264 Y386
• 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	A	G112 S113 Y144 H145 G146 D245 I247 A248 K274	G112 S113 Y144 H145 G146 D235 I237 A238 K264
BS02	KAP	A	Y17 W52 Y144 K274 R391 F393	Y17 W52 Y144 K264 R379 F381

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:1qj3, PDBe:1qj3, PDBj:1qj3
• PDBsum: 1qj3
• PubMed: 10452893
• UniProt: P12995|BIOA_ECOLI Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (Gene Name=bioA)