Structure of PDB 3m83 Chain F

Receptor sequence
>3m83F (length=325) Species: 2336 (Thermotoga maritima) [Search protein sequence]
HMAFFDLPLEELKKYRPERYEEKDFDEFWEETLAESEKFPLDPVFERMES
HLKTVEAYDVTFSGYRGQRIKGWLLVPKLEEEKLPCVVQYIGYNGGRGFP
HDWLFWPSMGYICFVMDTRGQGSGWLKGDTPDYPEGPVDPQYPGFMTRGI
LDPRTYYYRRVFTDAVRAVEAAASFPQVDQERIVIAGGSQGGGIALAVSA
LSKKAKALLCDVPFLCHFRRAVQLVDTHPYAEITNFLKTHRDKEEIVFRT
LSYFDGVNFAARAKIPALFSVGLMDNICPPSTVFAAYNYYAGPKEIRIYP
YNNHEGGGSFQAVEQVKFLKKLFEK
3D structure
PDB3m83 Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima.
ChainF
Resolution2.12 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S188 Q189 D274 H303
Catalytic site (residue number reindexed from 1) S189 Q190 D275 H304
Enzyme Commision number 3.1.1.41: cephalosporin-C deacetylase.
3.1.1.72: acetylxylan esterase.
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 CA F K22 E26 K23 E27
BS02 ACT F Q140 P142 G143 F144 R147 Q141 P143 G144 F145 R148
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046555 acetylxylan esterase activity
GO:0046872 metal ion binding
GO:0047739 cephalosporin-C deacetylase activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0005976 polysaccharide metabolic process
GO:0030245 cellulose catabolic process
GO:0045491 xylan metabolic process
GO:1901266 cephalosporin C metabolic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:3m83, PDBe:3m83, PDBj:3m83
PDBsum3m83
PubMed22411095
UniProtQ9WXT2|CAH_THEMA Cephalosporin-C deacetylase (Gene Name=axeA)

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