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1X9D

Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue

Functional Information from GO Data
ChainGOidnamespacecontents
A0004571molecular_functionmannosyl-oligosaccharide 1,2-alpha-mannosidase activity
A0005509molecular_functioncalcium ion binding
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AGLU330

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305
ChainResidueDetails
AASP463
AGLU599

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P31723
ChainResidueDetails
AGLU570

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P32906
ChainResidueDetails
ATHR688

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dl2
ChainResidueDetails
AARG334
AASP463
AGLU599
AGLU330

site_idMCSA1
Number of Residues4
DetailsM-CSA 19
ChainResidueDetails
AGLU330steric role
AARG334steric role
AASP463electrostatic stabiliser, proton acceptor, proton donor
AGLU599increase nucleophilicity, proton acceptor, proton donor

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PDB entries from 2025-06-11

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