Structure of PDB 6lpi Chain B

Receptor sequence

>6lpiB (length=539) Species: 83333 (Escherichia coli K-12)

STRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILA
RHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAIADARLDSIPLIC
ITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRI
AQSGRPGPVWIDIPKDVQTAVFEIETQPAMAEKAAAPAFSEESIRDAAAM
INAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGMLPKAHPLS
LGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVD
IDRAELGKIKQPHVAIQADVDDVLAQLIPLVEAQPRAEWHQLVADLQRED
PLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGL
GTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKI
ILMNNEALGLVHQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLPQ
ASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANTEMV

3D structure

• PDB: 6lpi Molecular architecture of the acetohydroxyacid synthase holoenzyme.
• Chain: B
• Resolution: 2.849 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): I34 G36 G37 S38 I39 E60 C83 F122 Q123 E124 K172 M263 A290 V391 G417 M419 D444 N471 A473 L474 L476 V477 Q480
• Catalytic site (residue number reindexed from 1): I27 G29 G30 S31 I32 E53 C76 F115 Q116 E117 K165 M256 A283 V375 G401 M403 D428 N455 A457 L458 L460 V461 Q464
• 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	FAD	B	R162 G219 G220 G221 T243 L244 M245 L261 M263 H264 G283 A284 R285 D287 R289 A290 D307 I308 D326 V327 M396 G414	R155 G212 G213 G214 T236 L237 M238 L254 M256 H257 G276 A277 R278 D280 R282 A283 D300 I301 D319 V320 M380 G398
BS02	TPP	B	G392 Q393 H394 G417 M419 G443 D444 G445 S446 M449 N471 A473 L474 G475 L476 V477	G376 Q377 H378 G401 M403 G427 D428 G429 S430 M433 N455 A457 L458 G459 L460 V461
BS03	MG	B	D444 N471	D428 N455
BS04	TPP	B	E60 C83 P86	E53 C76 P79

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0003984 acetolactate synthase activity
• GO:0005515 protein binding
• GO:0016740 transferase activity
• GO:0030976 thiamine pyrophosphate binding
• GO:0046872 metal ion binding
• GO:0050660 flavin adenine dinucleotide binding

Biological Process

• GO:0008652 amino acid biosynthetic process
• GO:0009082 branched-chain amino acid biosynthetic process
• GO:0009097 isoleucine biosynthetic process
• GO:0009099 L-valine biosynthetic process

Cellular Component

• GO:0005948 acetolactate synthase complex

External links

• PDB: RCSB:6lpi, PDBe:6lpi, PDBj:6lpi
• PDBsum: 6lpi
• PubMed: 32538427
• UniProt: P08142|ILVB_ECOLI Acetolactate synthase isozyme 1 large subunit (Gene Name=ilvB)