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1FMI

CRYSTAL STRUCTURE OF HUMAN CLASS I ALPHA1,2-MANNOSIDASE

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 Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1C
ChainResidue
ATHR688
AHOH699
AHOH700
AHOH701
AHOH702
AHOH703
AHOH704

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 698S
ChainResidue
AHOH946
AARG500
AHIS501

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2S
ChainResidue
ATRP299
AARG304
ALYS435
AHIS497
AHOH904

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 3S
ChainResidue
ATRP269
ATRP313
ALYS317
AHOH1061

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
APHE366

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305
ChainResidueDetails
ALEU499
ASER635

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P31723
ChainResidueDetails
ATYR606

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
APHE366steric role
ASER370steric role
ALEU499electrostatic stabiliser, proton acceptor, proton donor
ASER635increase nucleophilicity, proton acceptor, proton donor

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PDB entries from 2024-11-06

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