Structure of PDB 5mlz Chain A Binding Site BS02

Receptor Information

>5mlz Chain A (length=355) Species: 186497 (Pyrococcus furiosus DSM 3638)

FQSMKVSVIIPTYNERENLEELFSRIDNALQGLNYEIVVVDDDSPDRTWE
KAQELSSKYPVKVIRRTKEKGLSSAVIRGFKEASGDVFVVMDADLQHPPE
VIPKLIEAIKNGSDIAIGSRYVKGGKVENWPFYRKLISKGAIMVGRIALP
KIRDIKDPVSGFFALRKEVVEGVELNPIGFKILMEILIKGKYSKVVEVPF
TFGIRARGESKLKGKTIFEYLRHIYRLMKWEGEIDRIVKFSIVGLSGILV
NEGFLWLFVNLGIPKEIAVIPAVELSILNNFFWNDIWTFKDIRRGSIFSR
LLKFHIAALSGAVVNFIVYWILLFLGIHYLIANLVGIVLSFGVRYVINRH
VTWAT

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 5mlz Chain A Residue 402

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5mlz Structural basis for dolichylphosphate mannose biosynthesis.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): D91 Q93
• Binding residue (residue number reindexed from 1): D94 Q96
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.4.1.83: dolichyl-phosphate beta-D-mannosyltransferase.

Gene Ontology

Molecular Function

• GO:0004582 dolichyl-phosphate beta-D-mannosyltransferase activity
• GO:0016757 glycosyltransferase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0000271 polysaccharide biosynthetic process
• GO:0006486 protein glycosylation
• GO:0006488 dolichol-linked oligosaccharide biosynthetic process
• GO:0006506 GPI anchor biosynthetic process
• GO:0019348 dolichol metabolic process
• GO:0035269 protein O-linked mannosylation

Cellular Component

• GO:0005886 plasma membrane
• GO:0016020 membrane

External links

• PDB: RCSB:5mlz, PDBe:5mlz, PDBj:5mlz
• PDBsum: 5mlz
• PubMed: 28743912
• UniProt: Q8U4M3|DPM1_PYRFU Dolichol-phosphate mannosyltransferase (Gene Name=PF0058)