Structure of PDB 1kre Chain B

Receptor sequence
>1kreB (length=475) Species: 5077 (Penicillium citrinum) [Search protein sequence]
SNQAKADAVKEAFQHAWNGYMKYAFPHDELTPVSNGHADSRNGWGASAVD
ALSTAVIMGKADVVNAILEHVADIDFSKTSDTVSLFETTIRYLAGMLSGY
DLLQGPAKNLVDNQDLIDGLLDQSRNLADVLKFAFDTPSGVPYNNINITS
HGNDGATTNGLAVTGTLVLEWTRLSDLTGDEEYAKLSQKAESYLLKPQPS
SSEPFPGLVGSSININDGQFADSRVSWNGGDDSFYEYLIKMYVYDPKRFE
TYKDRWVLAAESTIKHLKSHPKSRPDLTFLSSYSNRNYDLSSQHLTCFDG
GSFLLGGTVLDRQDFIDFGLELVDGCEATYNSTLTKIGPDSWGWDPKKVP
SDQKEFYEKAGFYISSGSYVLRPEVIESFYYAHRVTGKEIYRDWVWNAFV
AINSTCRTDSGFAAVSDVNKANGGSKYDNQESFLFAEVMKYSYLAHSEDA
AWQVQKGGKNTFVYNTEAHPISVAR
3D structure
PDB1kre Structure of Penicillium citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and Golgi class I enzymes.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E122 R126 D267 E409
Catalytic site (residue number reindexed from 1) E87 R91 D232 E374
Enzyme Commision number 3.2.1.113: mannosyl-oligosaccharide 1,2-alpha-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 B K423 Y426 K388 Y391
BS02 DMJ B R407 E409 F468 E472 T501 E502 R372 E374 F433 E437 T466 E467
Gene Ontology
Molecular Function
GO:0004571 mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
GO:0005509 calcium ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1kre, PDBe:1kre, PDBj:1kre
PDBsum1kre
PubMed11714724
UniProtP31723|MAN12_PENCI Mannosyl-oligosaccharide alpha-1,2-mannosidase (Gene Name=MSDC)

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