Structure of PDB 3h3k Chain A

Receptor sequence
>3h3kA (length=528) Species: 1388 (Alicyclobacillus acidocaldarius subsp. acidocaldarius) [Search protein sequence]
KSIFYNQVGYLISGDKRFWIQAHEPQPFALRTPEGQAVFAGMTKPVGGNW
YVGDFTALRVPGTYTLTVGTLEARVVIHRRAYRDVLEAMLRFFDYQLCGV
VLPEDEAGPWAHGACHTSDAKVFGTERALACPGGWHDAGDYGKYTVPAAK
AVADLLLAHEYFPAALAHVRPMRSVHRAPHLPPALEVAREEIAWLLTMQD
PATGGVYHKVTTPSFPPLDTRPEDDDAPLVLSPISYAATATFCAAMAHAA
LVYRPFDPALSSCCADAARRAYAWLGAHEMQPFHNPDGILTGEYGDAELR
DELLWASCALLRMTGDSAWARVCEPLLDLDLPWELGWADVALYGVMDYLR
TPRAAVSDDVRNKVKSRLLRELDALAAMAESHPFGIPMRDDDFIWGSNMV
LLNRAMAFLLAEGVGVLHPAAHTVAQRAADYLFGANPLGQCYVTGFGQRP
VRHPHHRPSVADDVDHPVPGMVVGGPNRHLQDEIARAQLAGRPAMEAYID
HQDSYSTNEVAVYWNSPAVFVIAALLEA
3D structure
PDB3h3k Crystal structures of A. acidocaldarius endoglucanase Cel9A in complex with Cello-oligosaccharides: strong -1 and -2 subsites mimic cellobiohydrolase activity
ChainA
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) D143 D146 Y300 E515
Catalytic site (residue number reindexed from 1) D137 D140 Y294 E509
Enzyme Commision number 3.2.1.4: cellulase.
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 A A144 D146 G298 Y300 W401 E515 A138 D140 G292 Y294 W395 E509
BS02 BGC A W343 W401 Y519 W337 W395 Y513
BS03 BGC A H461 E515 H455 E509
BS04 CA A D302 E304 D307 E308 A344 D296 E298 D301 E302 A338
BS05 ZN A C104 C121 H122 H142 C98 C115 H116 H136
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3h3k, PDBe:3h3k, PDBj:3h3k
PDBsum3h3k
PubMed19729024
UniProtQ9AJS0

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