Structure of PDB 2q28 Chain A

Receptor sequence

>2q28A (length=550) Species: 83333 (Escherichia coli K-12) [Search protein sequence]

LQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHE
QSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALANATVNGFPMIMISG
SSDRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVS
VSGRPGGVYLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSA
ISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSMAKGILED
THPLSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIE
PQEIDSNRPIAVPVVGDIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQ
NAQKMHEKLSTDTQPLNYFNALSAVRDVLRENQDIYLVNEGANTLDNARN
IIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTSGSPVVAIEGDSAFGFSG
MEIETICRYNLPVTIVIFNNGGIYRGDGVDLSGAGAPSPTDLLHHARYDK
LMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPAAGTESGHIT

3D structure

PDB

2q28 New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli.

Chain

Resolution

1.74 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	V29 G31 I32 P33 V34 E54 V77 Y118 E119 E120 A168 L285 G395 G421 M423 D447 N474 G476 I477 R479 G480 V483 P544
Catalytic site (residue number reindexed from 1)	V25 G27 I28 P29 V30 E50 V73 Y114 E115 E116 A164 L281 G391 G417 M419 D443 N470 G472 I473 R475 G476 V479 P540
Enzyme Commision number	4.1.1.8: oxalyl-CoA 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	D447 N474 G476	D443 N470 G472
BS02	TPP	A	Y372 G395 A396 N397 T398 M423 G446 D447 S448 A449 F452 N474 G476 I477 Y478	Y368 G391 A392 N393 T394 M419 G442 D443 S444 A445 F448 N470 G472 I473 Y474
BS03	ADP	A	R158 G219 K220 G221 M245 G278 R280 D302 I303 D321 I322	R154 G215 K216 G217 M241 G274 R276 D298 I299 D317 I318

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0000287	magnesium ion binding
GO:0003824	catalytic activity
GO:0008949	oxalyl-CoA decarboxylase activity
GO:0016831	carboxy-lyase activity
GO:0030976	thiamine pyrophosphate binding
GO:0042802	identical protein binding
GO:0043531	ADP binding
GO:0046872	metal ion binding

	Biological Process
GO:0001561	fatty acid alpha-oxidation
GO:0019752	carboxylic acid metabolic process
GO:0033611	oxalate catabolic process
GO:0071468	cellular response to acidic pH

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:2q28, PDBe:2q28, PDBj:2q28
PDBsum	2q28
PubMed	20553497
UniProt	P0AFI0\|OXC_ECOLI Oxalyl-CoA decarboxylase (Gene Name=oxc)

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