Structure of PDB 6wo1 Chain A

Receptor sequence
>6wo1A (length=551) Species: 5207 (Cryptococcus neoformans) [Search protein sequence]
GLDYSFIGLSGGQIFQEMMLRHDVKQVFGYPGGAILPVFDAIYNSPHFEF
VLPRHEQGAGHMAEGYARVSGKPGVVLVTSGPGATNVITPMQDALSDGVP
MVVFCGQVATNLIGSDAFQEADVVGISRSCTKWNVMVKDIAELPRRINEA
FKIATTGRPGPVLVDLPKDVTAAILRTPIPAPLPGDADLITEAAQMINKA
KRPIIFAGNGVLSSPEGPKLLKELSDKGRIPVTTTLQGLGAFDERDEKSL
HMIGMHGSAYANFAMQEADVLIALGVRFDDRVTGKVDTFAPAAKAAAAEG
RGGIIHFEIQPKNINKIVEGQIPVLGDVVASLGELVPQIEAVDRSAWIGR
CKATKERYPFTYTPSQEGQKLKPQEVVQELDRQAEALGKEKFVISTGVGQ
HQMWACQYYRWTEPRSWVSSGGLGTMGFGLPSAIGAKVAAPEKYVIDIDG
DASFSMTAMELATASQYDIGVKVLLFNNETNPDFVKLSESMGAKGLRCTK
LEDLPRMMKEFLEYDGKRPIVLECLVSSEHVYPMIPAGKALHEQLLHPLL
R
3D structure
PDB6wo1 Structures of fungal and plant acetohydroxyacid synthases.
ChainA
Resolution3.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y147 G149 G150 A151 I152 E173 T196 F235 Q236 E237 K285 M396 V423 V539 G565 M567 D592 N619
Catalytic site (residue number reindexed from 1) Y30 G32 G33 A34 I35 E56 T79 F118 Q119 E120 K168 M255 V282 V398 G424 M426 D451 N478
Enzyme Commision number 2.2.1.6: acetolactate synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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: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:0005739 mitochondrion
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:6wo1, PDBe:6wo1, PDBj:6wo1
PDBsum6wo1
PubMed32640464
UniProtQ96VZ6

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