Structure of PDB 6efg Chain D

Receptor sequence
>6efgD (length=537) Species: 284590 (Kluyveromyces lactis NRRL Y-1140) [Search protein sequence]
SEITLGRYLFERLKQVEVQTIFGLPGDFNLSLLDNIYEVPGMRWAGNANE
LNAAYAADGYARLKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGV
PSVHTLGNGDFTVFHRMSSNISETTAMITDINTAPAEIDRCIRTTYVSQR
PVYLGLPANLVDLTVPASLLDTPIDLSLKPNDPEAEEEVIENVLQLIKEA
KNPVILADACCSRHDAKAETKKLIDLTQFPAFVTPMGKGSIDEKHPRFGG
VYVGTLSSPAVKEAVESADLVLSVGALSYKTKNIVEFHSDYTKIRSATFP
GVQMKFALQKLLTKVADAAKGYKPVPVPSEPEHNEAVADSTPLKQEWVWT
QVGEFLREGDVVITETGTSAFGINQTHFPNNTYGISQVLWGSIGFTTGAT
LGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNND
GYTIERLIHGETAQYNCIQNWQHLELLPTFGAKDYEAVRVSTTGEWNKLT
TDEKFQDNTRIRLIEVMLPTMDAPSNLVKQAQLTAAT
3D structure
PDB6efg The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis. Implications for the substrate activation mechanism of this enzyme.
ChainD
Resolution2.04 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) L25 G27 D28 F29 N30 E51 T73 H115 L117 G118 A169 T266 T388 G413 I415 D444 N471 G473 Y474 I476 E477 I480 T542
Catalytic site (residue number reindexed from 1) L24 G26 D27 F28 N29 E50 T72 H104 L106 G107 A158 T255 T366 G391 I393 D422 N449 G451 Y452 I454 E455 I458 T520
Enzyme Commision number 4.1.1.1: pyruvate 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 TPP D T390 I415 G443 G445 S446 N471 G473 Y474 T475 I476 E477 T368 I393 G421 G423 S424 N449 G451 Y452 T453 I454 E455
BS02 MG D D444 N471 G473 D422 N449 G451
BS03 TPP D P26 E51 V76 P25 E50 V75
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004737 pyruvate decarboxylase activity
GO:0016831 carboxy-lyase activity
GO:0030976 thiamine pyrophosphate binding
GO:0046872 metal ion binding
Biological Process
GO:0000949 aromatic amino acid family catabolic process to alcohol via Ehrlich pathway
Cellular Component
GO:0005634 nucleus
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6efg, PDBe:6efg, PDBj:6efg
PDBsum6efg
PubMed
UniProtQ12629|PDC1_KLULA Pyruvate decarboxylase (Gene Name=PDC1)

[Back to BioLiP]