Structure of PDB 4nrr Chain B

Receptor sequence
>4nrrB (length=415) Species: 4839 (Rhizomucor miehei) [Search protein sequence]
GSEFAFVKIASDGKGFTRYGEPYLIRGANYWQGMNLGADDCSGGDRKRME
LEIKQMAEMGINNLRVMASSEGPDDQPYRMRPSMMPQPGKYNEGVFVGLD
YLLDTMDRYNMTAVMTLGNFWQWSGGFGQYVAWITGNQTIPYPVGDVTYD
EFTQFAARFYNDSEIAPKANKLFKDHIYTVQNRRNTVNGKIYKEDPVIMS
WQIANAPQEAPASWFEEISTFIKKGAPKHLVSAGLESKLDEYDFDRAHDH
KNIDYTTCHCWVENWGIYDPADPDGLPHANEYMHDFLESRSKWAAQLNKP
IVMEEFGMARDAWRNPEDETYKYLPSTPTSHKDEYYQKAFNQIVSLASNR
SFSGSNFWAYGGEGRSTYPPNPYGMVWLGDPPHEPHGWYSVYSNDTTVQI
IKDYNANLLKVQKEL
3D structure
PDB4nrr Structural insights into the substrate specificity and transglycosylation activity of a fungal glycoside hydrolase family 5 beta-mannosidase.
ChainB
Resolution2.4 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.2.1.78: mannan endo-1,4-beta-mannosidase.
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 FRU B W117 Y145 E232 W261 W121 Y149 E236 W265
BS02 BMA B W119 N201 W257 E301 W354 P377 E380 Y385 W123 N205 W261 E305 W358 P381 E384 Y389
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004567 beta-mannosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016985 mannan endo-1,4-beta-mannosidase activity

View graph for
Molecular Function
External links
PDB RCSB:4nrr, PDBe:4nrr, PDBj:4nrr
PDBsum4nrr
PubMed25372687
UniProtA0A075C6T6

[Back to BioLiP]