Structure of PDB 2q5l Chain A

Receptor sequence
>2q5lA (length=538) Species: 192 (Azospirillum brasilense) [Search protein sequence]
VPRGSHMKLAEALLRALKDRGAQAMFGIPGDFALPFFKVAEETQILPLHT
LSHEPAVGFAADAAARYSSTLGVAAVTYGAGAFNMVNAVAGAYAEKSPVV
VISGAPGTTEGNAGLLLTLDTQFQVFKEITVAQARLDDPAKAPAEIARVL
GAARAQSRPVYLEIPRNMVNAEVEPVGDDPAWPVDRDALAACADEVLAAM
RSATSPVLMVCVEVRRYGLEAKVAELAQRLGVPVVTTFMGRGLLADAPTP
PLGTYIGVAGDAEITRLVEESDGLFLLGAILSDTNFAVSQRKIDLRKTIH
AFDRAVTLGYHTYADIPLAGLVDALLERLPPSDRTTRGKEPHAYPTGLQA
DGEPIAPMDIARAVNDRVRAGQEPLLIAADMGDCLFTAMDMIDAGLMAPG
YYAGMGFGVPAGIGAQCVSGGKRILTVVGDGAFQMTGWELGNCRRLGIDP
IVILFNNASWEMLRTFQPESAFNDLDDWRFADMAAGMGGDGVRVRTRAEL
KAALDKAFATRGRFQLIEAMIPRGVLSDTLARFVQGQK
3D structure
PDB2q5l Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I22 G24 D25 F26 A27 E48 T71 T117 L118 R165 V257 N284 M380 A402 M404 D429 N456 S458 W459 M461 L462 F465 R522
Catalytic site (residue number reindexed from 1) I28 G30 D31 F32 A33 E54 T77 T118 L119 R166 V258 N285 M381 A403 M405 D430 N457 S459 W460 M462 L463 F466 R523
Enzyme Commision number 4.1.1.74: indolepyruvate decarboxylase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016831 carboxy-lyase activity
GO:0030976 thiamine pyrophosphate binding
GO:0047434 indolepyruvate decarboxylase activity
Biological Process
GO:0009851 auxin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2q5l, PDBe:2q5l, PDBj:2q5l
PDBsum2q5l
PubMed17905741
UniProtP51852|DCIP_AZOBR Indole-3-pyruvate decarboxylase (Gene Name=ipdC)

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