Structure of PDB 3bcd Chain A

Receptor sequence
>3bcdA (length=585) Species: 373903 (Halothermothrix orenii H 168) [Search protein sequence]
SLFLIESEPSTGASVSKNLTEIILIFSNDINKVSQLALTDLITDSDIQGI
DYNIEGNKVIINNFSLEPTCNYRLSYEVIDIYDNHLQGYIEFLVNQSNYP
QIPDQEVNHTILQAFYWEMNTGEYATEHPEEANLWNLLAERAPELAEAGF
TAVWLPPANKGMAGIHDVGYGTYDLWDLGEFDQKGTVRTKYGTKGELENA
IDALHNNDIKVYFDAVLNHRMGADYAETVLLDENSRDKPGQYIKAWTGFN
FPGRNGEYSNFTWNGQCFDGTDWDDYSKESGKYLFDEKSWDWTYNWDEDY
LMGADVDYENEAVQNDVIDWGQWIINNIDFDGFRLDAVKHIDYRFIDKWM
SAVQNSSNRDVFFVGEAWVEDVDDLKGFLDTVGNPDLRVFDFPLRSFFVD
MLNGAYMADLRNAGLVNSPGYENRAVTFVDNHDTDRDEGSYTVSIYSRKY
QAYAYILTRAEGVPTVYWKDYYIWEMKEGLDKLLTARRYYAYGPGYEVDN
NDADIYSYVRSGFPDVAGDGLVLMISDGTSGNVAGKWINSRQPDTEFYDL
TGHIKEHVTTDSEGYGNFKVIKSEDKGWSIWVPVE
3D structure
PDB3bcd Crystal Structure of the Polyextremophilic alpha-Amylase AmyB from Halothermothrix orenii: Details of a Productive Enzyme-Substrate Complex and an N Domain with a Role in Binding Raw Starch
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D350 E380 D447
Catalytic site (residue number reindexed from 1) D336 E366 D433
Enzyme Commision number 3.2.1.98: glucan 1,4-alpha-maltohexaosidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033927 glucan 1,4-alpha-maltohexaosidase 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:3bcd, PDBe:3bcd, PDBj:3bcd
PDBsum3bcd
PubMed18387632
UniProtB8CZ54

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