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1FO3

CRYSTAL STRUCTURE OF HUMAN CLASS I ALPHA1,2-MANNOSIDASE IN COMPLEX WITH KIFUNENSINE

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 PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 700
ChainResidue
ATHR688
AKIF704
AHOH705
AHOH708
AHOH709
AHOH710

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AARG500
AHIS501

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
ALYS435
AHIS497
AHOH1081
AHOH1084
AARG304

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 703
ChainResidue
ATRP269
ATRP313
ALYS317
AHOH1051
AHOH1090

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE KIF A 704
ChainResidue
AARG334
AASP463
ALEU525
AARG597
APRO598
AGLU599
APHE659
AGLU663
ATHR688
AGLU689
ACA700
AHOH709
AHOH710
AHOH712
AHOH713
AHOH714
AHOH715
AHOH716

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P31723","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P32906","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

243531

PDB entries from 2025-10-22

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