Structure of PDB 5ahk Chain A

Receptor sequence

>5ahkA (length=555) Species: 380021 (Pseudomonas protegens)

MKASDAVAKILADNNVLYGFELIGGMITHLVDSINLLGKTKLVSMHHEQG
AAFAASAVSRVTHHKTLGLALATSGPGATNLITGIADCWLDSHPCIFLTG
QVNTHELKGKRDIRQQGFQELDSVALVTSITKYAYQIKSADELVPCLRKA
IQIAKEGRPGPVLLDIPMDIQRADIDEALLNNPSIAMSDLDFIINKLQNA
KKPLLLIGGGAVNSSGFQKWLEQIELRGIPYVASLKGAEKIKASDLYLGM
LGAYGTRAANHAVQNCDLLLVLGSRMDVRQTGAQPEDFARNAEIIQIDLQ
EGQLNNRVIADFSYQIELSEYFSRFSPLQIPVNNDWSVWTALLKEKFRVT
FIDEYTTWNLSPFGLFTQLNKLTERVALDYILDVGNNQMWAAHTLRLNAQ
QAMHHSGGLGSMGFAIPAAIGACYAGKKPIIVITGDGGAQLNIQELDIIA
RDKLPILTIVMNNHSLGMVRGFQEMYFEGRNSSTYWNGYTSQFKKIGEAY
RVESKTIISMQAFSSALESFLESPRPLLLEVSMSDARECRPRLEYGRAID
QQSPR

3D structure

• PDB: 5ahk The Crystal Structure of the Acetohydroxy Acid Synthase Pf5 from Pseudomonas Protegens
• Chain: A
• Resolution: 1.55 Å

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 A253 Q280 V384 G410 M412 D436 N463 S465 L466 M468 V469 F472 D535
• 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	TPP	A	V394 G395 N396 N397 G420 M422 D446 G447 G448 N473 S475 L476 G477 M478 V479	V384 G385 N386 N387 G410 M412 D436 G437 G438 N463 S465 L466 G467 M468 V469
BS02	FAD	A	R158 G218 G219 G220 S244 L245 M260 L261 Y264 G283 S284 R285 D287 R289 Q290 D308 L309 Q313 E327 L328 M399 G417	R158 G208 G209 G210 S234 L235 M250 L251 Y254 G273 S274 R275 D277 R279 Q280 D298 L299 Q303 E317 L318 M389 G407
BS03	MG	A	D446 N473 S475	D436 N463 S465
BS04	TPP	A	I23 E48 P76	I23 E48 P76

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

External links

• PDB: RCSB:5ahk, PDBe:5ahk, PDBj:5ahk
• PDBsum: 5ahk
• UniProt: Q4K6F7