Structure of PDB 1v26 Chain A

Receptor sequence
>1v26A (length=489) Species: 274 (Thermus thermophilus) [Search protein sequence]
AFPSTMMDEELNLWDFLERAAALFGRKEVVSRLHTGEVHRTTYAEVYQRA
RRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLS
PKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGY
LAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLA
ASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPA
SLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPR
SLIARFERMGVEVRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKT
GLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSA
LTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENAAVVA
IPHPKWQERPLAVVGFAKWQLPDAYLKRALREQYKNYYG
3D structure
PDB1v26 Structural Basis of the Substrate-specific Two-step Catalysis of Long Chain Fatty Acyl-CoA Synthetase Dimer
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T184 H204 H230 T327 E328 K439 W444
Catalytic site (residue number reindexed from 1) T177 H197 H223 T320 E321 K432 W437
Enzyme Commision number 6.2.1.3: long-chain-fatty-acid--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 MG A T184 E328 T177 E321
BS02 AMP A G302 S303 A304 G323 Y324 G325 L326 T327 D418 K435 K439 W444 G295 S296 A297 G316 Y317 G318 L319 T320 D411 K428 K432 W437
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004467 long-chain fatty acid-CoA ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0001676 long-chain fatty acid metabolic process
GO:0006631 fatty acid metabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1v26, PDBe:1v26, PDBj:1v26
PDBsum1v26
PubMed15145952
UniProtQ5SKN9|LCFCS_THET8 Long-chain-fatty-acid--CoA ligase (Gene Name=TTHA0604)

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