Structure of PDB 5e2j Chain A

Receptor sequence
>5e2jA (length=530) Species: 1388 (Alicyclobacillus acidocaldarius subsp. acidocaldarius) [Search protein sequence]
PKSIFYNQVGYLISGDKRFWIQAHEPQPFALRTPEGQAVFAGMTKPVGGN
WYVGDFTALRVPGTYTLTVGTLEARVVIHRRAYRDVLEAMLRFFDYQLCG
VVLPEDEAGPWAHGACHTSDAKVFGTERALACPGGWHDAGDYGKYTVPAA
KAVADLLLAHEYFPAALAHVRPMRSVHRAPHLPPALEVAREEIAWLLTMQ
DPATGGVYHKVTTPSFPPLDTRPEDDDAPLVLSPISYAATATFCAAMAHA
ALVYRPFDPALSSCCADAARRAYAWLGAHEMQPFHNPDGILTGEYGDAEL
RDELLWASCALLRMTGDSAWARVCEPLLDLDLPWELGWADVALYGVMDYL
RTPRAAVSDDVRNKVKSRLLRELDALAAMAESHPFGIPMRDDDFIWGSNM
VLLNRAMAFLLAEGVGVLHPAAHTVAQRAADYLFGANPLGQCYVTGFGQR
PVRHPHHRPSVAADVDHPVPGMVVGGPNRHLQDEIARAQLAGRPAMEAYI
DHQDSYSTNEVAVYWNSPAVFVIAALLEAR
3D structure
PDB5e2j Polarity Alteration of a Calcium Site Induces a Hydrophobic Interaction Network and Enhances Cel9A Endoglucanase Thermostability.
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) D138 D141 Y295 E510
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 CA A D302 E304 D307 E308 A344 D297 E299 D302 E303 A339
BS02 ZN A C104 C121 H122 H142 C99 C116 H117 H137
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:5e2j, PDBe:5e2j, PDBj:5e2j
PDBsum5e2j
PubMed26729722
UniProtQ9AJS0

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