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Crystal structure of human CPSF30 in complex with HFIP1

Analyse Crystal structure of human CPSF30 in complex with HFIP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7K95
Type
protein
Length
123 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Isoform 2 of cleavage and polyadenylation specificity factor subunit 4; Pre-mRNA…
UniProt
Q6UN15
Ligands
ZN

Structure

x-ray diffraction · 3 distinct chains · 38% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIsoform 2 of cleavage and polyadenylation specificity factor subunit 4protein5330% helix, 11% strand—
BPre-mRNA 3'-end-processing factor FIP1protein3949% helix, 3% strandQ6UN15
CPre-mRNA 3'-end-processing factor FIP1protein3139% helix, 3% strandQ6UN15

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A

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

Interfaces

3 interfaces between chains.

  • A–B · 819 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 517 Ų buried · 12 hydrogen bonds · protein-protein
  • B–C · 335 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7K95 · Crystal structure of human CPSF30 in complex with hFip1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6UN15 · AlphaFold monomer V2.0 prediction for pre-mRNA 3'-end-processing factor FIP1 (Q6UN15) · a predicted model of the same protein · chain B against A, TM-score 0.88

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