Structure of PDB 4zh5 Chain B

Receptor sequence
>4zh5B (length=425) Species: 6356 (Perinereis brevicirris) [Search protein sequence]
QYNYREVLQKSILFYAAQRSGQLPGNNPIDWRDDSALDDQGNGGEDLTGG
WYDAGDHVKFGLPMAWTATTLIWGMIDLANGYGGDRNDAMQSVRWALDYF
MKCHVSDNELYGQVGDGHADHAYWGRPEEMTMDRPAWSLTPSAPGSDLAG
ETAAALAAGSILFSDSDASYANQLLDHARTIYDFAYNNRGIYSESIPNAA
DFYRSSAYEDELCWGALWLYRATGEQDYMDKANEFLPQGRPWAFSWDSKE
AGSLVLLTSFGNSNARAQLEDFLQSWFPGGDIHYTPLGLAWRDTWGSLRY
SANSAFIALLAAEEGVLTSQARTFARAQLDYMLGSTGRSFVVGFGTNPPL
RPHHRAASCPDMPASCGWDQASDPAPNPQVLDGALVGGPDDQDNYNDDRQ
DYISNEVACDYNAGFQGALAGILQL
3D structure
PDB4zh5 Biophysical and structural characterisation of the endoglucanase from Perinereis brevicirris
ChainB
Resolution1.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D61 D64 Y211 E414
Catalytic site (residue number reindexed from 1) D53 D56 Y203 E406
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 BGC B W376 Y410 W368 Y402
BS02 BGC B H129 H361 R363 Y410 E414 H121 H353 R355 Y402 E406
BS03 BGC B D398 D399 D390 D391
BS04 CA B A215 D218 E219 D255 A207 D210 E211 D247
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4zh5, PDBe:4zh5, PDBj:4zh5
PDBsum4zh5
PubMed
UniProtF2Z7L1

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