Structure of PDB 4rlf Chain B

Receptor sequence
>4rlfB (length=519) Species: 1076 (Rhodopseudomonas palustris) [Search protein sequence]
VTPPPEKFNFAEHLLQTNRVRPDKTAFVDDISSLSFAQLEAQTRQLAAAL
RAIGVKREERVLLLMLDGTDWPVAFLGAIYAGIVPVAVNTLLTADDYAYM
LEHSRAQAVLVSGALHPVLKAALTKSDHEVQRVIVSRPAAPLEPGEVDFA
EFVGAHAPLEKPAATQADDPAFWLYSSGSTGRPKGVVHTHANPYWTSELY
GRNTLHLREDDVCFSAAKLFFAYGLGNALTFPMTVGATTLLMGERPTPDA
VFKRWLGGVGGVKPTVFYGAPTGYAGMLAAPNLPSRDQVALRLASSAGEA
LPAEIGQRFQRHFGLDIVDGIGSTEMLHIFLSNLPDRVRYGTTGWPVPGY
QIELRGDGGGPVADGEPGDLYIHGPSSATMYWGNRAKSRDTFQGGWTKSG
DKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIEATLVQHPGVLEAAVVG
VADEHGLTKPKAYVVPRPGQTLSETELKTFIKDRLAPYKYPRSTVFVAEL
PKTATGKIQRFKLREGVLG
3D structure
PDB4rlf Kinetically and Crystallographically Guided Mutations of a Benzoate CoA Ligase (BadA) Elucidate Mechanism and Expand Substrate Permissivity.
ChainB
Resolution1.73 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 3SK B A227 Y228 G303 I326 G327 S328 H333 A222 Y223 G298 I321 G322 S323 H328
BS02 4MA B A221 P251 P253 G274 A275 G278 A216 P246 P248 G269 A270 G273
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:4rlf, PDBe:4rlf, PDBj:4rlf
PDBsum4rlf
PubMed26378464
UniProtQ93TK0

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