Structure of PDB 4k2i Chain B

Receptor sequence
>4k2iB (length=439) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
MQKQVKISGKSKENMSLLKHLKGDVQGKELVIEDSIVNERWKQVLKEKID
IEHDLFNYQKNREISKVPFLPVDRLITNDEVEDILNTLTEVLPTGKFTSG
PYLEQFEKVLSTYLHKRYVIATSSGTDAIMIGLLALGLNPGDEVIMPANS
FSATENAVLASGGVPIYVDINPQTFCIDPDKIEEAITPYTKFILPVHLYG
KHSDMQHIRQIANRYKLKVIEDACQGIGLTDLGKYADITTLSFNPYKNFG
VCGKAGAIATDNEELAKKCIQFSYHGFEVNVKNKKVINFGFNSKMDNLQA
AIGLERMKYLSLNNFKRLFLADRYITQLAELQNKGYIELPELSEDHVWHL
FPIKVRTEDRADIMTKLNEDFGVQTDVYYPILSHMQKTPLVQDKYAGLQL
VHTEKAHSQVLHLPLYPSFTLEEQDRVMEGLFHVIKQEI
3D structure
PDB4k2i The Structure of NtdA, a Sugar Aminotransferase Involved in the Kanosamine Biosynthetic Pathway in Bacillus subtilis, Reveals a New Subclass of Aminotransferases.
ChainB
Resolution2.225 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F151 D222 Q225 N244 K247 K284 K294
Catalytic site (residue number reindexed from 1) F151 D222 Q225 N244 K247 K284 K294
Enzyme Commision number 2.6.1.104: 3-dehydro-glucose-6-phosphate--glutamate 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 PMP B G125 T126 F151 D222 C224 Q225 S242 K247 G125 T126 F151 D222 C224 Q225 S242 K247
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0000271 polysaccharide biosynthetic process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4k2i, PDBe:4k2i, PDBj:4k2i
PDBsum4k2i
PubMed24097983
UniProtO07566|NTDA_BACSU 3-oxo-glucose-6-phosphate:glutamate aminotransferase (Gene Name=ntdA)

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