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Structure of HDCP1A in complex with proline rich sequence of PNRC2

Analyse Structure of HDCP1A in complex with proline rich sequence of PNRC2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4B6H
Type
protein
Length
256 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MRNA-decapping enzyme 1A; Proline-rich nuclear receptor coactivator 2
EC
3.-.-.-
UniProt
Q9NPI6, Q9NPJ4
Pockets
2 · best druggability 0.37

Structure

x-ray diffraction · 4 distinct chains · 21% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMRNA-decapping enzyme 1A (EC 3.-.-.-)protein12926% helix, 47% strandQ9NPI6
BMRNA-decapping enzyme 1A (EC 3.-.-.-)protein10013% helix, 54% strandQ9NPI6
CProline-rich nuclear receptor coactivator 2protein1421% helix, 0% strandQ9NPJ4
DProline-rich nuclear receptor coactivator 2protein1323% helix, 0% strandQ9NPJ4

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11060.370.7523empty
2680.350.7619empty

Interfaces

3 interfaces between chains.

  • A–C · 733 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 669 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 361 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 4B6H · Structure of hDcp1a in complex with proline rich sequence of PNRC2 · the same entry in another collection · chain D against D, TM-score 1.00
  • Q9NPI6 · AlphaFold monomer V2.0 prediction for mRNA-decapping enzyme 1A (Q9NPI6) · a predicted model of the same protein · chain B against A, TM-score 0.98
  • Q9NPJ4 · AlphaFold monomer V2.0 prediction for proline-rich nuclear receptor coactivator 2 (Q9NPJ4) · a predicted model of the same protein · chain D against A, TM-score 0.47

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