Structure of PDB 4cvq Chain B

Receptor sequence
>4cvqB (length=404) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
SPIEKSSKLENVCYDIRGPVLKEAKRLEEEGNKVLKLNIGNPAPFGFDAP
DEILVDVIRNLPTAQGYCDSKGLYSARKAIMQHYQARGMRDVTVEDIYIG
NGVSELIVQAMQALLNSGDEMLVPAPDYPLWTAAVSLSSGKAVHYLCDES
SDWFPDLDDIRAKITPRTRGIVIINPNNPTGAVYSKELLMEIVEIARQHN
LIIFADEIYDKILYDDAEHHSIAPLAPDLLTITFNGLSKTYRVAGFRQGW
MVLNGPKKHAKGYIEGLEMLASMRLCANVPAQHAIQTALGGYQSISEFIT
PGGRLYEQRNRAWELINDIPGVSCVKPRGALYMFPKIDAKRFNIHDDQKM
VLDFLLQEKVLLVQGTAFNWPWPDHFRIVTLPRVDDIELSLSKFARFLSG
YHQL
3D structure
PDB4cvq Structural analysis and mutant growth properties reveal distinctive enzymatic and cellular roles for the three major L-alanine transaminases of Escherichia coli.
ChainB
Resolution2.11 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.2: alanine 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 G103 V104 S105 Y129 D207 I209 Y210 S239 K240 R248 G102 V103 S104 Y128 D206 I208 Y209 S238 K239 R247
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004021 L-alanine:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006523 alanine biosynthetic process
GO:0006974 DNA damage response
GO:0008652 amino acid biosynthetic process
GO:0009058 biosynthetic process
GO:0019272 L-alanine biosynthetic process from pyruvate
GO:0030632 D-alanine biosynthetic process
GO:0046677 response to antibiotic
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:4cvq, PDBe:4cvq, PDBj:4cvq
PDBsum4cvq
PubMed25014014
UniProtP0A959|ALAA_ECOLI Glutamate-pyruvate aminotransferase AlaA (Gene Name=alaA)

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