Structure of PDB 5dx6 Chain A

Receptor sequence
>5dx6A (length=541) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
PVRQWAHGADLVVSQLEAQGVRQVFGIPGAKIDKVFDSLLDSSIRIIPVR
HEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVAL
GGAVKRADKAKMDTVAMFSPVTKYAIEVTAPDALAEVVSNAFRAAEQGRP
GSAFVSLPQDVVDGPVSGKVLPAPQMGAAPDDAIDQVAKLIAQAKNPIFL
LGLMASQPENSKALRRLLETSHIPVTSTYQAAGAVNQDNFSRFAGRVGLF
NNQAGDRLLQLADLVICIGYSPVEYEPAMWNSGNATLVHIDVLPAYEERN
YTPDVELVGDIAGTLNKLAQNIDHRLVLSPQAAEILRDRQHQRELLDRRG
AQLNQFALHPLRIVRAMQDIVNSDVTLTVDMGSFHIWIARYLYSFRARQV
MISNGQQTMGVALPWAIGAWLVNPERKVVSVSGDGGFLQSSMELETAVRL
KANVLHLIWVDNGYNMVAIQEEKKYQRLSGVEFGPMDFKAYAESFGAKGF
AVESAEALEPTLRAAMDVDGPAVVAIPVDYRDNPLLMGQLH
3D structure
PDB5dx6 Characterization of Acetolactate Synthase from Klebsiella pneumoniae
ChainA
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I32 G34 A35 K36 I37 E57 T80 Q169 L262 E289 M394 Q420 M422 D447 D474 G476 Y477 M479 V480 Q483 Y543
Catalytic site (residue number reindexed from 1) I27 G29 A30 K31 I32 E52 T75 Q159 L249 E276 M381 Q407 M409 D434 D461 G463 Y464 M466 V467 Q470 Y530
Enzyme Commision number 2.2.1.6: acetolactate synthase.
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 MG A D447 D474 G476 D434 D461 G463
BS02 MG A S129 T132 S119 T122
BS03 5GY A M394 G395 S396 F397 Q420 M422 G446 D447 G448 D474 G476 Y477 N478 Y543 M381 G382 S383 F384 Q407 M409 G433 D434 G435 D461 G463 Y464 N465 Y530
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003984 acetolactate synthase activity
GO:0016740 transferase activity
GO:0030976 thiamine pyrophosphate binding
GO:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0009097 isoleucine biosynthetic process
GO:0009099 L-valine biosynthetic process
GO:0019752 carboxylic acid metabolic process
GO:0034077 butanediol metabolic process
Cellular Component
GO:0005948 acetolactate synthase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5dx6, PDBe:5dx6, PDBj:5dx6
PDBsum5dx6
PubMed
UniProtP27696|ILVB_KLEPN Acetolactate synthase, catabolic (Gene Name=budB)

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