Structure of PDB 5k8f Chain C

Receptor sequence
>5k8fC (length=651) Species: 235443 (Cryptococcus neoformans var. grubii H99) [Search protein sequence]
HHVHPLPDSVPESEDLFAPPPRMQGKEGRPKPHIGPNYESYVKEWAKTVG
PNSDEWWAAKARETLDWYDDFKTVRAGGFEHGDVQWFPEGTLNAAYNCLD
RHYYKNPKKTAIIYEADEPSESREVSYEELMQETCRVANVLKSYGVKKGD
AVSIYLPMTWQAAAAFLACARIGAIHSAVFAGFSAESLRDRVNDCECKVL
ITTDEGRRGGKTIATKQIVDAALQQCPLVENVLVLRRTGNKVPMTEGRDK
WWDEECAKMPAYCPCERMASEDPLFILYTSKPKGVVHSTAGYLLGTALTL
KYVFDAHPDDRFACMADIGWITGHSYIIYGPLANGITTAVFESTPVYPTP
SRYWDFVDKWKATQLYTAPTAIRLLRRMGEDHVKNHDLSSLRVLGSVGEP
INPEAWHWYNDFAGKNQCAIVDTYWMTETGSISIAPLPGAISTKPGSATF
PFFGMDVDIIDPQTGQVLEGNDVEGVLVARRPWPSIARTVYRDHKRYLET
YMKPYPGYFFFGDGAARDYDGYMWIKGRVDDVINVSGHRLSTAEVESALI
LHKGVAETAVVGCADDLTGQAVYAFVTMKPEFDLKATKEADLSKELAIQV
RKVIGPFAAPKKIYLVSDLPKTRSGKIMRRVLRKIVAGEPQIVEEVKQKV
T
3D structure
PDB5k8f Crystal structure of Acetyl-CoA Synthetase in complex with ATP and Acetyl-AMP from Cryptococcus neoformans H99
ChainC
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T289 T441 E442 N548 R553 K640
Catalytic site (residue number reindexed from 1) T279 T427 E428 N534 R539 K626
Enzyme Commision number 6.2.1.1: acetate--CoA ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003987 acetate-CoA ligase activity
GO:0005524 ATP binding
GO:0016208 AMP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006085 acetyl-CoA biosynthetic process
GO:0019427 acetyl-CoA biosynthetic process from acetate
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5k8f, PDBe:5k8f, PDBj:5k8f
PDBsum5k8f
PubMed
UniProtJ9VFT1

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