Structure of PDB 6lpi Chain A

Receptor sequence

>6lpiA (length=531) Species: 83333 (Escherichia coli K-12)

KRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHE
QGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAIADARLDSIPLICITG
QVPASEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWI
DIPKDVQTAVFEIQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGG
GVINAPARVRELAEKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGVRSTN
YILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPH
VAIQADVDDVLAQLIPLVEAQPRAEWHQLVADLQREFPCPPLSHYGLINA
VAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAA
IGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGL
VHQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNDPQASLQEIIN
RPGPALIHVRIDAEEKVYPMVPPGAANTEMV

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): I34 G36 G37 S38 I39 E60 C83 E124 K172 M263 A290 V391 G417 M419 D444 N471 A473 L474 L476 V477 Q480
• Catalytic site (residue number reindexed from 1): I24 G26 G27 S28 I29 E50 C73 E106 K154 M243 A270 V365 G391 M393 D418 N445 A447 L448 L450 V451 Q454
• 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	A	R162 G219 G220 G221 T243 L244 M245 L261 M263 G283 A284 R285 R289 A290 D307 I308 A325 D326 V327 M396 G414	R144 G199 G200 G201 T223 L224 M225 L241 M243 G263 A264 R265 R269 A270 D287 I288 A305 D306 V307 M370 G388
BS02	TPP	A	V391 G392 Q393 H394 M419 G445 S446 M449 N471 L474 G475 L476 V477	V365 G366 Q367 H368 M393 G419 S420 M423 N445 L448 G449 L450 V451
BS03	MG	A	D444 N471	D418 N445
BS04	TPP	A	E60 C83 P86	E50 C73 P76

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)