Structure of PDB 2q27 Chain B

Receptor sequence
>2q27B (length=545) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHE
QSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALANATVNGFPMIMISG
SSDRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVS
VSGRPGGVYLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSA
ISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSMAKGILED
THPLSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIE
PQEIDSNRPIAVPVVGDIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQ
NAQKMHEKLSTDTQPLNYFNALSAVRDVLRENQDIYLVNEGANTLDNARN
IIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTSGSPVVAIEGDSAFGFSG
MEIETICRYNLPVTIVIFNNGGIYRGDGVDLSGAGAPSPTDLLHHARYDK
LMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPAAGTE
3D structure
PDB2q27 New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli.
ChainB
Resolution2.12 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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)		 Binding affinity
BS01 MG B D447 N474 G476 D443 N470 G472
BS02 TPP B Y372 A396 N397 T398 G421 M423 G446 D447 S448 A449 F452 N474 G476 I477 Y478 Y368 A392 N393 T394 G417 M419 G442 D443 S444 A445 F448 N470 G472 I473 Y474
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:2q27, PDBe:2q27, PDBj:2q27
PDBsum2q27
PubMed20553497
UniProtP0AFI0|OXC_ECOLI Oxalyl-CoA decarboxylase (Gene Name=oxc)

[Back to BioLiP]