Structure of PDB 2d2o Chain B

Receptor sequence
>2d2oB (length=585) Species: 2026 (Thermoactinomyces vulgaris) [Search protein sequence]
MLLEAIFHEAKGSYAYPISETQLRVRLRAKKGDVVRCEVLYADRYASPEE
ELAHALAGKAGSDERFDYFEALLECSTKRVKYVFLLTGPQGEAVYFGETG
FSAERSKAGVFQYAYIHRSEVFTTPEWAKEAVIYQIFPERFANGDPSNDP
PGTEQWAKDARPRHDSFYGGDLKGVIDRLPYLEELGVTALYFTPIFASPS
HHKYDTADYLAIDPQFGDLPTFRRLVDEAHRRGIKIILDAVFNHAGDQFF
AFRDVLQKGEQSRYKDWFFIEDFPVSKTSRTNYETFAVQVPAMPKLRTEN
PEVKEYLFDVARFWMEQGIDGWRLNVANEVDHAFWREFRRLVKSLNPDAL
IVGEIWHDASGWLMGDQFDSVMNYLFRESVIRFFATGEIHAERFDAELTR
ARMLYPEQAAQGLWNLLDSHDTERFLTSCGGNEAKFRLAVLFQMTYLGTP
LIYYGDEIGMAGATDPDCRRPMIWEEKEQNRGLFEFYKELIRLRHRLASL
TRGNVRSWHADKQANLYAFVRTVQDQHVGVVLNNRGEKQTVLLQVPESGG
KTWLDCLTGEEVHGKQGQLKLTLRPYQGMILWNGR
3D structure
PDB2d2o Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D239 R323 N325 E354 H420 D421
Catalytic site (residue number reindexed from 1) D239 R323 N325 E354 H420 D421
Enzyme Commision number 3.2.1.135: neopullulanase.
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 GLC B F286 E354 F286 E354
BS02 GLC B Y204 H244 F286 N325 E354 H420 D421 Y204 H244 F286 N325 E354 H420 D421
BS03 GLC B H202 Y204 D465 R469 H202 Y204 D465 R469
BS04 GLC B H164 D465 H164 D465
BS05 CA B N143 D145 P146 N148 D149 G169 D171 N143 D145 P146 N148 D149 G169 D171
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031216 neopullulanase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2d2o, PDBe:2d2o, PDBj:2d2o
PDBsum2d2o
PubMed16564038
UniProtQ08751|NEPU2_THEVU Neopullulanase 2 (Gene Name=tvaII)

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