Structure of PDB 3dlp Chain X

Receptor sequence
>3dlpX (length=504) Species: 206162 (Alcaligenes sp. AL3007) [Search protein sequence]
MQTVNEMLRRAATRAPDHCALAVPARGLRLTHAELRARVEAVAARLHADG
LRPQQRVAVVAPNSADVVIAILALHRLGAVPALLNPRLKSAELAELIKRG
EMTAAVIAVGRQVADAIFQSGSGARIIFLGDLVRDGEPYSYGPPIEDPQR
EPAQPAFIFYTSGTTGLPKAAIIPQRAAESRVLFMSTQVGLRHGRHNVVL
GLMPLYHVVGFFAVLVAALALDGTYVVVEEFRPVDALQLVQQEQVTSLFA
TPTHLDALAAAAAHAGSSLKLDSLRHVTFAGATMPDAVLETVHQHLPGEK
VNIYGTTEAMNSLYMRQPKTGTEMAPGFFSEVRIVRIGGGVDEIVANGEE
GELIVAASDSAFVGYLNQPQATAEKLQDGWYRTSDVAVWTPEGTVRILGR
VPDMIISGGENIHPSEIERVLGTAPGVTEVVVIGLADQRWGQSVTACVVP
RLGETLSADALDTFCRSSELADFKRPKRYFILDQLPKNALNKVLRRQLVQ
QVSS
3D structure
PDB3dlp The mechanism of domain alternation in the acyl-adenylate forming ligase superfamily member 4-chlorobenzoate: coenzyme A ligase
ChainX
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.2.1.33: 4-chlorobenzoate--CoA ligase.
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 174 X F184 H207 V209 I303 G305 T306 M310 N311 F184 H207 V209 I303 G305 T306 M310 N311
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0016874 ligase activity
GO:0031956 medium-chain fatty acid-CoA ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006631 fatty acid metabolic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3dlp, PDBe:3dlp, PDBj:3dlp
PDBsum3dlp
PubMed19320426
UniProtQ8GN86

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