Structure of PDB 3hwx Chain I

Receptor sequence

>3hwxI (length=554) Species: 83333 (Escherichia coli K-12)

MSVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTLLTLAAAENSAFIHH
THFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIEAGLTGEKL
ILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVS
TIDHALGTLHAGGVHINCPFAEPLYMDDTGLSWQQRLGDWWQDDKPWLRE
APRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDV
LSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCE
PEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKRQPWCVEIPRL
AEQAMQAVIARRDAFGEAQLAHRICDYLPEQGQLFVGNSLVVRLIDALSQ
LPAGYPVYSNRGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNAL
ALLRQVSAPLVLIVVNNNGGQIFSLLPTPQSERERFYLMPQNVHFEHAAA
MFELKYHRPQNWQELETAFADAWRTPTTTVIEMVVNDTDGAQTLQQLLAQ
VSHL

3D structure

• PDB: 3hwx Structural and functional analysis of Vitamin K2 synthesis protein MenD.
• Chain: I
• Resolution: 2.6 Å

Enzymatic activity

• Enzyme Commision number: 2.2.1.9: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase.

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	I	S391 L392 I418 D419 G441 D442 L443 S444 N469 G471 G472 Q473 I474	S389 L390 I416 D417 G439 D440 L441 S442 N467 G469 G470 Q471 I472
BS02	MG	I	D442 N469 G471	D440 N467 G469
BS03	TPP	I	P30 E55 A82	P30 E55 A82

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0016740 transferase activity
• GO:0030145 manganese ion binding
• GO:0030976 thiamine pyrophosphate binding
• GO:0042803 protein homodimerization activity
• GO:0046872 metal ion binding
• GO:0070204 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity

Biological Process

• GO:0009234 menaquinone biosynthetic process

External links

• PDB: RCSB:3hwx, PDBe:3hwx, PDBj:3hwx
• PDBsum: 3hwx
• PubMed: 19703421
• UniProt: P17109|MEND_ECOLI 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (Gene Name=menD)