Structure of PDB 3i6e Chain G

Receptor sequence
>3i6eG (length=356) Species: 89184 (Ruegeria pomeroyi) [Search protein sequence]
LEQKIIAMDLWHLALPVCEIVVLRLVAEGGAEGFGEASPWAVFTGTPEAS
YAALDRYLRPLVIGRRVGDRVAIMDEAARAVAHCTEAKAALDSALLDLAG
RISNLPVWALLGGKCRDTIPLSCSIANPDFDADIALMERLRADGVGLIKL
KTGFRDHAFDIMRLELIARDFPEFRVRVDYNQGLEIDEAVPRVLDVAQFQ
PDFIEQPVRAHHFELMARLRGLTDVPLLADESVYGPEDMVRAAHEGICDG
VSIKIMKSGGLTRAQTVARIAAAHGLMAYGGDMFEAGLAHLAGTHMIAAT
PEITLGCEFYQASYFLNEDILETPFRVEAGQVIVPDGPGLGARADPEKLE
HYAVRR
3D structure
PDB3i6e Crystal structure of muconate lactonizing enzyme from Ruegeria pomeroyi.
ChainG
Resolution1.7 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) S143 K168 K170 D198 Y199 N200 Q201 E224 D249 E250 S251 K273 Y298 G300 D301 M302 C326 E327 F328
Catalytic site (residue number reindexed from 1) S124 K149 K151 D179 Y180 N181 Q182 E205 D230 E231 S232 K254 Y279 G281 D282 M283 C307 E308 F309
Enzyme Commision number 5.5.1.1: muconate cycloisomerase.
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 G D198 E224 D249 D179 E205 D230
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0018849 muconate cycloisomerase activity
GO:0018850 chloromuconate cycloisomerase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process
GO:0009063 amino acid catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3i6e, PDBe:3i6e, PDBj:3i6e
PDBsum3i6e
PubMed
UniProtQ5LM96

[Back to BioLiP]