Structure of PDB 3ele Chain D

Receptor sequence
>3eleD (length=398) Species: 39491 (Agathobacter rectalis) [Search protein sequence]
GMVVNESMYQLGSVRSAIRELFEYGKKRAAIVGKENVYDFSIGNPSIPAP
QIVNDTIKELVTDYDSVALHGYTSAQGDVETRAAIAEFLNNTHGTHFNAD
NLYMTMGAAASLSICFRALTSDAYDEFITIAPYFPEYKVFVNAAGARLVE
VPADTEHFQIDFDALEERINAHTRGVIINSPNNPSGTVYSEETIKKLSDL
LEKKSKEIGRPIFIIADEPYREIVYDGIKVPFVTKYYDNTLVCYSYSKSL
SLPGERIGYVLVPDEVYDKAELYAAVCGAGRALGYVCAPSLFQKMIVKCQ
GATGDINAYKENRDLLYEGLTRIGYHCFKPDGAFYMFVKALEDDSNAFCE
KAKEEDVLIVAADGFGCPGWVRISYCVDREMIKHSMPAFEKIYKKYNK
3D structure
PDB3ele Crystal structure of Amino Transferase (RER070207001803) from Eubacterium rectale at 2.10 A resolution
ChainD
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F133 I207 R209 K247
Catalytic site (residue number reindexed from 1) F134 I208 R210 K248
Enzyme Commision number 2.6.1.-
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 G106 A107 N178 N182 D216 P218 Y219 S244 S246 K247 R255 G107 A108 N179 N183 D217 P219 Y220 S245 S247 K248 R256
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ele, PDBe:3ele, PDBj:3ele
PDBsum3ele
PubMed
UniProtD0VX02

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