Structure of PDB 3vm7 Chain A

Receptor sequence
>3vm7A (length=470) Species: 5041 (Malbranchea cinnamomea) [Search protein sequence]
ATPDEWRSRSIYQVLTDRFARGDGSPDAPCDTGARKYCGGNYRGLISQLD
YIQGMGFDSVWISPITKQFEDDWNGAPYHGYWQTDLYALNEHFGTEEDLR
ALADELHARGMFLMVDVVINHNGWPGDAASIDYSQFNPFNSSDYYHPPCE
INYDDQTSVEQCWLYTGANALPDLKTEDPHVSQVHNDWIADLVSKYSIDG
LRIDTTKHVDKPAIGSFNDAAGVYAVGEVYHGDPAYTCPYQDWVDGVLNF
PVYYPLIDAFKSPSGTMWSLVDNINKVFQTCNDPRLLGTFSENHDIPRFA
SYTQDLALAKNVLAFTILFDGIPIVYAGQEQQYSGDSDPYNREALWLSGF
NTDAPLYKHIAACNRIRSHAVSNDDAYITTPTDIKYSDDHTLALVKGAVT
TVLTNAGANAGETTVTVEATGYASGEQVTDVLSCESIAASDGGRLSVTLN
QGLPRVFFPTDALAGSGLCE
3D structure
PDB3vm7 A Novel Multifunctional alpha-Amylase from the Thermophilic Fungus Malbranchea cinnamomea: Biochemical Characterization and Three-Dimensional Structure.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D137 R223 D225 E249 H315 D316
Catalytic site (residue number reindexed from 1) D116 R202 D204 E228 H294 D295
Enzyme Commision number 3.2.1.1: alpha-amylase.
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 A N141 E181 D194 H229 N120 E160 D173 H208
BS02 GLC A T226 H229 E249 Y251 D316 T205 H208 E228 Y230 D295
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3vm7, PDBe:3vm7, PDBj:3vm7
PDBsum3vm7
PubMed23536251
UniProtK9L8F3

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