Structure of PDB 2man Chain A

Receptor sequence
>2manA (length=298) Species: 2021 (Thermobifida fusca) [Search protein sequence]
ATGLHVKNGRLYEANGQEFIIRGVSHPHNWYPQHTQAFADIKSHGANTVR
VVLSNGVRWSKNGPSDVANVISLCKQNRLICMLEVHDTTGYGEQSGASTL
DQAVDYWIELKSVLQGEEDYVLINIGNEPYGNDSATVAAWATDTSAAIQR
LRAAGFEHTLVVDAPNWGQDWTNTMRNNADQVYASDPTGNTVFSIHMYGV
YSQASTITSYLEHFVNAGLPLIIGEFGHDNPDEDTIMAEAERLKLGYIGW
SWSGNGGGVEYLDMVYNFDGDNLSPWGERIFYGPNGIASTAKEAVIFG
3D structure
PDB2man High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R50 N127 E128 H196 Y198 E225 W254
Catalytic site (residue number reindexed from 1) R50 N127 E128 H196 Y198 E225 W250
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 MAN A H86 N259 G260 H86 N255 G256
BS02 BMA A W30 W59 W30 W59
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016985 mannan endo-1,4-beta-mannosidase activity
Biological Process
GO:0000272 polysaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2man, PDBe:2man, PDBj:2man
PDBsum2man
PubMed9817845
UniProtQ9ZF13

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