MolNFT v1 · #6422 · protein

The crystal structure of trans-activation domain of the sporulation response regulator, SPO0A

1FC3: “The crystal structure of trans-activation domain of the sporulation response regulator, SPO0A”. X-ray diffraction, 3 pockets (best druggability 0.34). MolNFT v1 #6422 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1FC3
Type: protein
Length: 336 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SPO0A
UniProt: P52934
Pockets: 3 · best druggability 0.34

Structure

x-ray diffraction · 3 distinct chains · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SPO0A	protein	119	71% helix, 0% strand	P52934
B	SPO0A	protein	101	78% helix, 0% strand	P52934
C	SPO0A	protein	116	76% helix, 0% strand	P52934

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.34	0.76	11	empty
2	66	0.34	0.76	14	empty
3	65	0.29	0.74	15	empty

Interfaces

2 interfaces between chains.

A–C · 531 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 501 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

1FC3 · The crystal structure of trans-activation domain of the sporulation response regulator… · the same entry in another collection · chain A against A, TM-score 1.00
P52934 · AlphaFold monomer V2.0 prediction for stage 0 sporulation protein a (P52934) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 P52934
Elsewhere: RCSB PDB 1FC3 · PDBe 1FC3 · UniProt P52934

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