MolNFT v1 · #37680 · protein

Structural basis for the specific recognition of methylated histone H3 lysine 4 by the wd-40 protein WDR5

2G99 · Wd-repeat protein 5: “Structural basis for the specific recognition of methylated histone H3 lysine 4 by the wd-40 protein WDR5”. X-ray diffraction, 4 pockets (best druggability 0.83). MolNFT v1 #37680 on GenesisL1: 3D structure…

PDB: 2G99
Type: protein
Length: 618 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Wd-repeat protein 5; Histone H3
UniProt: P61964
Pockets: 4 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Wd-repeat protein 5	protein	304	0% helix, 51% strand	P61964
C, D	Histone H3	protein	5	0% helix, 0% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	830	0.83	0.86	74	empty
2	492	0.73	0.82	44	empty
3	194	0.56	0.79	28	empty
4	61	0.40	0.80	18	empty

Interfaces

3 interfaces between chains.

B–C · 508 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 490 Å² buried · 1 hydrogen bond · protein-protein
A–D · 449 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (methylation).

Compared structures

2G99 · Structural basis for the specific recognition of methylated histone H3 lysine 4 by the… · the same entry in another collection · chain A against A, TM-score 1.00

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 P61964
Elsewhere: RCSB PDB 2G99 · PDBe 2G99 · UniProt P61964

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