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Crystal structure of rpff

Analyse Crystal structure of rpff in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3M6N
Type
protein
Length
796 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rpff protein
UniProt
Q7CLS3
Pockets
6 · best druggability 0.77

Structure

x-ray diffraction · 3 distinct chains · 53% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARpff proteinprotein26453% helix, 16% strandQ7CLS3
BRpff proteinprotein26853% helix, 16% strandQ7CLS3
CRpff proteinprotein26453% helix, 16% strandQ7CLS3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1860.770.9828empty
2800.760.9827empty
39470.720.7660empty
41410.690.9016empty
51590.640.8622empty

Interfaces

3 interfaces between chains.

  • B–C · 1015 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 1008 Ų buried · 11 hydrogen bonds · protein-protein
  • A–C · 1006 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 3M6N · Crystal structure of RpfF · the same entry in another collection · chain A against A, TM-score 1.00

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