Structure of PDB 5ahk Chain B

Receptor sequence

>5ahkB (length=546) Species: 380021 (Pseudomonas protegens) [Search protein sequence]

MKASDAVAKILADNNVLYGFELIGGMITHLVDSINLLGKTKLVSMHHEQG
AAFAASAVSRVTHHKTLGLALATSGPGATNLITGIADCWLDSHPCIFLTG
QVNTHELKGKRDIRQQGFQELDSVALVTSITKYAYQIKSADELVPCLRKA
IQIAKEGRPGPVLLDIPMDIQRADIDEALLNIAMSDLDFIINKLQNAKKP
LLLIGGGAVNSSGFQKWLEQIELRGIPYVASLKGAEKIKASDLYLGMLGA
YGTRAANHAVQNCDLLLVLGSRMDVRQTGAQPEDFARNAEIIQIDLQEGQ
LNNRVIADFSYQIELSEYFSRFSPLQIPVNNDWSVWTALLKEKFRVTFID
EYTTWNLSPFGLFTQLNKLTERVALDYILDVGNNQMWAAHTLRLNAQQAM
HHSGGLGSMGFAIPAAIGACYAGKKPIIVITGDGGAQLNIQELDIIARDK
LPILTIVMNNHSLGMVRGFSSTYWNGYTSQFKKIGEAYRVESKTIISMQA
FSSALESFLESPRPLLLEVSMSDARECRPRLEYGRAIDQQSPRHDG

3D structure

PDB

5ahk The Crystal Structure of the Acetohydroxy Acid Synthase Pf5 from Pseudomonas Protegens

Chain

Resolution

1.55 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	L22 G24 G25 M26 I27 E48 T73 K110 R111 F118 Q119 M168 A263 Q290 V394 G420 M422 D446 N473 S475 L476 M478 V479 F482 D545
Catalytic site (residue number reindexed from 1)	L22 G24 G25 M26 I27 E48 T73 K110 R111 F118 Q119 M168 A250 Q277 V381 G407 M409 D433 N460 S462 L463 M465 V466 F469 D523
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)
BS01	TPP	B	I23 E48 P76	I23 E48 P76
BS02	TPP	B	V394 G395 N396 N397 G420 M422 D446 G447 G448 N473 S475 L476 G477 M478	V381 G382 N383 N384 G407 M409 D433 G434 G435 N460 S462 L463 G464 M465
BS03	FAD	B	R158 G218 G219 G220 S244 L245 K246 M260 L261 Y264 G283 S284 R285 D287 R289 Q290 D308 L309 Q313 E327 L328 M399 G417	R158 G205 G206 G207 S231 L232 K233 M247 L248 Y251 G270 S271 R272 D274 R276 Q277 D295 L296 Q300 E314 L315 M386 G404
BS04	MG	B	D446 N473 S475	D433 N460 S462

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0000287	magnesium ion binding
GO:0003824	catalytic activity
GO:0003984	acetolactate synthase 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

	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:5ahk, PDBe:5ahk, PDBj:5ahk
PDBsum	5ahk
PubMed
UniProt	Q4K6F7

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