Structure of PDB 1krf Chain B

Receptor sequence

>1krfB (length=475) Species: 5077 (Penicillium citrinum)

SNQAKADAVKEAFQHAWNGYMKYAFPHDELTPVSNGHADSRNGWGASAVD
ALSTAVIMGKADVVNAILEHVADIDFSKTSDTVSLFETTIRYLAGMLSGY
DLLQGPAKNLVDNQDLIDGLLDQSRNLADVLKFAFDTPSGVPYNNINITS
HGNDGATTNGLAVTGTLVLEWTRLSDLTGDEEYAKLSQKAESYLLKPQPS
SSEPFPGLVGSSININDGQFADSRVSWNGGDDSFYEYLIKMYVYDPKRFE
TYKDRWVLAAESTIKHLKSHPKSRPDLTFLSSYSNRNYDLSSQHLTCFDG
GSFLLGGTVLDRQDFIDFGLELVDGCEATYNSTLTKIGPDSWGWDPKKVP
SDQKEFYEKAGFYISSGSYVLRPEVIESFYYAHRVTGKEIYRDWVWNAFV
AINSTCRTDSGFAAVSDVNKANGGSKYDNQESFLFAEVMKYSYLAHSEDA
AWQVQKGGKNTFVYNTEAHPISVAR

3D structure

• PDB: 1krf Structure of Penicillium citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and Golgi class I enzymes.
• Chain: B
• Resolution: 2.2 Å

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	KIF	B	L330 R407 P408 E409 F468 E472 T501 E502	L295 R372 P373 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

External links

• PDB: RCSB:1krf, PDBe:1krf, PDBj:1krf
• PDBsum: 1krf
• PubMed: 11714724
• UniProt: P31723|MAN12_PENCI Mannosyl-oligosaccharide alpha-1,2-mannosidase (Gene Name=MSDC)