Structure of PDB 1eix Chain A

Receptor sequence

>1eixA (length=231) Species: 562 (Escherichia coli)

VTNSPVVVALDYHNRDDALAFVDKIDPRDCRLKVGKEMFTLFGPQFVREL
QQRGFDIFLDLKFHDIPNTAAHAVAAAADLGVWMVNVHASGGARMMTAAR
EALVPFGKDAPLLIAVTVLTSMEASDLVDLGMTLSPADYAERLAALTQKC
GLDGVVCSAQEAVRFKQVFGQEFKLVTPGIRPQGSEAGDQRRIMTPEQAL
SAGVDYMVIGRPVTQSVDPAQTLKAINASLQ

3D structure

• PDB: 1eix Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K44 D71 K73 D76 T131 R222
• Catalytic site (residue number reindexed from 1): K33 D60 K62 D65 T120 R211
• Enzyme Commision number: 4.1.1.23: orotidine-5'-phosphate 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	BMQ	A	A20 D22 K44 K73 L130 T131 P189 R192 Q201 G221 R222	A9 D11 K33 K62 L119 T120 P178 R181 Q190 G210 R211	MOAD: Ki=8.8pM PDBbind-CN: -logKd/Ki=11.06,Ki=8.8pM
BS02	BMQ	A	D76 I77 T80	D65 I66 T69	MOAD: Ki=8.8pM PDBbind-CN: -logKd/Ki=11.06,Ki=8.8pM

Gene Ontology

Molecular Function

• GO:0004590 orotidine-5'-phosphate decarboxylase activity
• GO:0005515 protein binding
• GO:0016831 carboxy-lyase activity

Biological Process

• GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
• GO:0006221 pyrimidine nucleotide biosynthetic process
• GO:0015949 nucleobase-containing small molecule interconversion
• GO:0044205 'de novo' UMP biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1eix, PDBe:1eix, PDBj:1eix
• PDBsum: 1eix
• PubMed: 10757968
• UniProt: P08244|PYRF_ECOLI Orotidine 5'-phosphate decarboxylase (Gene Name=pyrF)