Structure of PDB 6m2t Chain D

Receptor sequence
>6m2tD (length=518) Species: 1076 (Rhodopseudomonas palustris) [Search protein sequence]
VTPPPEKFNFAEHLLQTNRVRPDKTAFVDDISSLSFAQLEAQTRQLAAAL
RAIGVKREERVLLLMLDGTDWPVAFLGAIYAGIVPVAVNTLLTADDYAYM
LEHSRAQAVLVSGALHPVLKAALTKSDHEVQRVIVSRPAAPLEPGEVDFA
EFVGAHAPLEKPAATQADDPAFWLYSSGSTGRPKGVVHTHANPYWTSELY
GRNTLHLREDDVCFSAAKLFFAYGLGNALTFPMTVGATTLLMGERPTPDA
VFKRWLGGVGGVKPTVFYGAPTGYAGMLAAPNLPSRDQVALRLASSAGEA
LPAEIGQRFQRHFGLDIVDGIGSTEMLAAFLSNLPDRVRYGTTGWPVPGY
QIELRGDGGGPVADGEPGDLYIHGPSSATMYWGNRAKSRDTFQGGWTKSG
DKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIEATLVQHPGVLEAAVVG
VADEHGLTKPKAYVVPRPGQTLSETELKTFIKDRLAPYKYPRSTVFVAEL
PKTATGKIQRFKLREGVL
3D structure
PDB6m2t The crystal structure of benzoate coenzyme A ligase double mutant (H333A/I334A) in complex with 2-methyl-thiazole-5 carboxylate-AMP
ChainD
Resolution2.14 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S181 T201 T329 E330 K427 Y432 K512
Catalytic site (residue number reindexed from 1) S176 T196 T324 E325 K422 Y427 K507
Enzyme Commision number ?
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 AMP D G303 E304 A305 G325 I326 S328 T329 D406 R421 K427 Y432 G298 E299 A300 G320 I321 S323 T324 D401 R416 K422 Y427
BS02 6V9 D Y228 A302 G327 S328 A333 Y223 A297 G322 S323 A328
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0005524 ATP binding
GO:0016405 CoA-ligase activity
GO:0016874 ligase activity
GO:0016878 acid-thiol ligase activity
Biological Process
GO:0044550 secondary metabolite biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6m2t, PDBe:6m2t, PDBj:6m2t
PDBsum6m2t
PubMed
UniProtQ93TK0

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