Structure of PDB 3mwc Chain A

Receptor sequence
>3mwcA (length=388) Species: 521045 (Kosmotoga olearia TBF 19.5.1) [Search protein sequence]
LTESARIDGVSLYEIVIPMKIPFQISSGTCYTRRSLVVEIREGDLFGYGE
SAPFEEPFYLGETLETTKVILKNHLLPMILGKEPLSIEEFNHLIKNGIRG
NHFARCGVENAYWDLIAKKNKISLKAMIEKKMKNLGVKQEYLASNNYIES
GAALGIPEDGRIETLIHQVEESLQEGYRRIKIKIKPGWDVEPLQETRRAV
GDHFPLWTDANSSFELDQWETFKAMDAAKCLFHEQPLHYEALLDLKELGE
RIETPICLDESLISSRVAEFVAKLGISNIWNIKIQRVGGLLEAIKIYKIA
TDNGIKLWGGTMPESGLGARFLISLASFRGFVFPADVAASEKWYGKGNDL
VENTMTDGKIYVPDEPGASFDMTLSHLEALGKKIWESQ
3D structure
PDB3mwc Crystal Structure of O-Succinylbenzoic Acid Synthetase from Kosmotoga Olearia
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F24 A154 K182 K184 D210 E235 D260 K284 T312 M313 D337
Catalytic site (residue number reindexed from 1) F23 A153 K181 K183 D209 E234 D259 K283 T311 M312 D336
Enzyme Commision number 4.2.1.113: o-succinylbenzoate 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 MG A D210 E235 D260 D209 E234 D259
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0043748 O-succinylbenzoate synthase activity
GO:0046872 metal ion binding
Biological Process
GO:0009234 menaquinone biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3mwc, PDBe:3mwc, PDBj:3mwc
PDBsum3mwc
PubMed
UniProtC5CFI0

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