Structure of PDB 2q5o Chain A

Receptor sequence

>2q5oA (length=529) Species: 192 (Azospirillum brasilense) [Search protein sequence]

HMKLAEALLRALKDRGAQAMFGIPGDFALPFFKVAEETQILPLHTLSHEP
AVGFAADAAARYSSTLGVAAVTYGAGAFNMVNAVAGAYAEKSPVVVISGA
PGTTEGNAGLLLHHQGRTLDTQFQVFKEITVAQARLDDPAKAPAEIARVL
GAARAQSRPVYLEIPRNMVNAEVEPVGDDPAWPVDRDALAACADEVLAAM
RSATSPVLMVCVEVRRYGLEAKVAELAQRLGVPVVTTFMGRGLLADAPTP
PLGTYIGVAGDAEITRLVEESDGLFLLGAILSDTNFAVSQRKIDLRKTIH
AFDRAVTLGYHTYADIPLAGLVDALLERLPPSPHAYPTGLQADGEPIAPM
DIARAVNDRVRAGQEPLLIAADMGDCLFTAMDMIDAGLMAPGYYAGMGFG
VPAGIGAQCVSGGKRILTVVGDGAFQMTGWELGNCRRLGIDPIVILFNNA
SWEMLRTFQPESAFNDLDDWRFADMAAGMGGDGVRVRTRAELKAALDKAF
ATRGRFQLIEAMIPRGVLSDTLARFVQGQ

3D structure

PDB

2q5o Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase.

Chain

Resolution

2.15 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 H112 H113 G115 R116 T117 L118 R165 V257 N284 M380 A402 M404 D429 N456 S458 W459 M461 L462 F465 R522
Catalytic site (residue number reindexed from 1)	I23 G25 D26 F27 A28 E49 T72 H113 H114 G116 R117 T118 L119 R166 V258 N285 M373 A395 M397 D422 N449 S451 W452 M454 L455 F458 R515
Enzyme Commision number	4.1.1.74: indolepyruvate decarboxylase.

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)
BS01	MG	A	D429 N456 S458	D422 N449 S451
BS02	TPW	A	D382 M404 G428 D429 G430 A431 N456 S458 W459 E460 M461 L462	D375 M397 G421 D422 G423 A424 N449 S451 W452 E453 M454 L455
BS03	PPY	A	G24 D25 H112 H113	G25 D26 H113 H114
BS04	PPY	A	R60 R214 R215 M238 G241 L395 M396 A397	R61 R215 R216 M239 G242 L388 M389 A390
BS05	TPW	A	P23 E48 A74	P24 E49 A75
BS06	PPY	A	T283 M461 F532	T284 M454 F525

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

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:2q5o, PDBe:2q5o, PDBj:2q5o
PDBsum	2q5o
PubMed	17905741
UniProt	P51852\|DCIP_AZOBR Indole-3-pyruvate decarboxylase (Gene Name=ipdC)

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