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MolNFT v1 · #37242 · protein

Crystal structure analysis of human rcd-1 conserved region

2FV2 · RCD1 required for cell DIFFERENTIATION1 homolog: “Crystal structure analysis of human rcd-1 conserved region”. X-ray diffraction, 1 ligand (MN), 9 pockets (best druggability 0.71). MolNFT v1 #37242 on GenesisL1: 3D structure…

PDB
2FV2
Type
protein
Length
1,069 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RCD1 required for cell DIFFERENTIATION1 homolog
Ligands
MN
Pockets
9 · best druggability 0.71

Structure

x-ray diffraction · 3 distinct chains · 74% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARCD1 required for cell DIFFERENTIATION1 homologprotein26775% helix, 1% strand—
BRCD1 required for cell DIFFERENTIATION1 homologprotein26677% helix, 0% strand—
C, DRCD1 required for cell DIFFERENTIATION1 homologprotein26871% helix, 0% strand—

Ligands and binding sites

  • MN · Manganese (II) ion · metal · chains A, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111190.710.7580empty
26280.620.7445empty
32040.600.8135empty
42500.570.7838empty
52480.540.7729empty

Interfaces

5 interfaces between chains.

  • C–D · 1030 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 994 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 332 Ų buried · 14 hydrogen bonds · protein-protein
  • A–D · 73 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 42 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2FV2 · Crystal Structure Analysis of human Rcd-1 conserved region · the same entry in another collection · chain A against A, TM-score 1.00

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