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Crystal structure of MS0802, C-myc-1 binding protein domain from homo sapiens

Analyse Crystal structure of MS0802, C-myc-1 binding protein domain from homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YY0
Type: protein
Length: 181 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-myc-binding protein
UniProt: Q99417

Structure

x-ray diffraction · 3 distinct chains · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C-myc-binding protein	protein	38	82% helix, 0% strand	Q99417
B, D	C-myc-binding protein	protein	53	77% helix, 0% strand	Q99417
C	C-myc-binding protein	protein	37	89% helix, 0% strand	Q99417

Interfaces

5 interfaces between chains.

A–B · 1162 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 1115 Å² buried · 1 hydrogen bond · protein-protein
A–C · 540 Å² buried · 5 hydrogen bonds · protein-protein
B–C · 12 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 12 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2YY0 · Crystal Structure of MS0802, c-Myc-1 binding protein domain from Homo sapiens · the same entry in another collection · chain A against A, TM-score 1.00
Q99417 · AlphaFold monomer V2.0 prediction for C-myc-binding protein (Q99417) · a predicted model of the same protein · chain C against A, TM-score 0.88

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q99417
Elsewhere: RCSB PDB 2YY0 · PDBe 2YY0 · UniProt Q99417

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