Structure of PDB 6rl5 Chain D

Receptor sequence
>6rl5D (length=417) Species: 290398 (Chromohalobacter israelensis DSM 3043) [Search protein sequence]
QILERMESEVRTYSRSFPTVFTEAKGARLHAEDGNQYIDFLAGAGTLNYG
HNHPKLKQALADYIASDGIVHGLDMWSAAKRDYLETLEEVILKPRGLDYK
VHLPGPTGTNAVEAAIRLARNAKGRHNIVTFTNGFHGVTMGALATTGNRK
FREATGGIPTQGASFMPFDGYMGEGVDTLSYFEKLLGDNSGGLDVPAAVI
IETVQGEGGINPAGIPWLQRLEKICRDHDMLLIVDDIQAGCGRTGKFFSF
EHAGITPDIVTNSKSLSGFGLPFAHVLMRPELDIWKPGQYNGTFRGFNLA
FVTAAAAMRHFWSDDTFERDVQRKGRVVEDRFQKLASFMTEKGHPASERG
RGLMRGLDVGDGDMADKITAQAFKNGLIIETSGHSGQVIKCLCPLTITDE
DLVGGLDILEQSVKEVF
3D structure
PDB6rl5 The crystal structure of the tetrameric DABA-aminotransferase EctB, a rate-limiting enzyme in the ectoine biosynthesis pathway.
ChainD
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S17 F138 D238 K267
Catalytic site (residue number reindexed from 1) S14 F135 D235 K264
Enzyme Commision number 2.6.1.76: diaminobutyrate--2-oxoglutarate 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 D G295 T296 G292 T293
BS02 PLP D G111 T112 F138 D238 I240 K267 G108 T109 F135 D235 I237 K264
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0045303 diaminobutyrate-2-oxoglutarate transaminase activity
GO:0047307 diaminobutyrate-pyruvate transaminase activity
Biological Process
GO:0009058 biosynthetic process
GO:0019491 ectoine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6rl5, PDBe:6rl5, PDBj:6rl5
PDBsum6rl5
PubMed32112674
UniProtQ9ZEU7|ECTB_CHRSD Diaminobutyrate--2-oxoglutarate transaminase (Gene Name=ectB)

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