Structure of PDB 3vpm Chain A Binding Site BS01

Receptor Information

>3vpm Chain A (length=286) Species: 9606 (Homo sapiens)

MGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEAVDLSKDIQ
HWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGF
QIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWI
GDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISR
DEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALPVKLIG
MNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFM

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: 3vpm Chain A Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3vpm Essential role of E106 in the proton-coupled electron transfer in human ribonucleotide reductase M2 subunit
• Resolution: 2.7 Å
• Binding residue (original residue number in PDB): R78 V81 T156
• Binding residue (residue number reindexed from 1): R14 V17 T92
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): Y176
• Catalytic site (residue number reindexed from 1): Y112
• Enzyme Commision number: 1.17.4.1: ribonucleoside-diphosphate reductase.

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity

Biological Process

• GO:0009263 deoxyribonucleotide biosynthetic process

External links

• PDB: RCSB:3vpm, PDBe:3vpm, PDBj:3vpm
• PDBsum: 3vpm
• UniProt: P31350|RIR2_HUMAN Ribonucleoside-diphosphate reductase subunit M2 (Gene Name=RRM2)