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Crystal structure of S. cerevisiae RFA1 N-ob domain mutant (K45E)

Analyse Crystal structure of S. cerevisiae RFA1 N-ob domain mutant (K45E) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5M1X
Type
protein
Length
518 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Replication factor a protein 1
UniProt
P22336
Pockets
6 · best druggability 0.73

Structure

x-ray diffraction · 4 distinct chains · 23% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReplication factor a protein 1protein13022% helix, 37% strandP22336
BReplication factor a protein 1protein12722% helix, 34% strandP22336
CReplication factor a protein 1protein12825% helix, 36% strandP22336
DReplication factor a protein 1protein13323% helix, 36% strandP22336

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15980.730.8084empty
21730.530.7923empty
31750.520.7925empty
41320.430.7624empty
51330.430.7623empty

Interfaces

5 interfaces between chains.

  • A–C · 632 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 529 Ų buried · 6 hydrogen bonds · protein-protein
  • A–D · 250 Ų buried · 1 hydrogen bond · protein-protein
  • C–D · 207 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 27 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

  • 5M1X · Crystal structure of S. cerevisiae Rfa1 N-OB domain mutant (K45E) · the same entry in another collection · chain D against D, TM-score 1.00
  • P22336 · AlphaFold monomer V2.0 prediction for replication factor a protein 1 (P22336) · a predicted model of the same protein · chain C against A, TM-score 0.94

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