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The crystal structure of human steroidogenic factor-1

Analyse The crystal structure of human steroidogenic factor-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZDT
Type: protein
Length: 495 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Steroidogenic factor 1; Nuclear receptor coactivator 2
UniProt: Q13285, Q15596
Ligands: PEF
Pockets: 8 · best druggability 0.84

Structure

x-ray diffraction · 4 distinct chains · 70% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Steroidogenic factor 1	protein	233	70% helix, 3% strand	Q13285
B	Steroidogenic factor 1	protein	239	71% helix, 3% strand	Q13285
P	Nuclear receptor coactivator 2	protein	12	75% helix, 0% strand	Q15596
Q	Nuclear receptor coactivator 2	protein	11	64% helix, 0% strand	Q15596

Ligands and binding sites

PEF · Di-palmitoyl-3-sn-phosphatidylethanolamine · ligand · 2 copies · chains A, B

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

Pockets

8 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	632	0.84	0.88	50	PEF
2	549	0.83	0.88	42	PEF
3	191	0.67	0.86	33	empty
4	192	0.48	0.76	28	empty
5	90	0.38	0.76	17	empty

Interfaces

2 interfaces between chains.

A–P · 590 Å² buried · 3 hydrogen bonds · protein-protein
B–Q · 539 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1ZDT · The Crystal Structure of Human Steroidogenic Factor-1 · the same entry in another collection · chain A against A, TM-score 1.00
Q13285 · AlphaFold monomer V2.0 prediction for steroidogenic factor 1 (Q13285) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 Q13285
Every structure of UniProt Q15596
Elsewhere: RCSB PDB 1ZDT · PDBe 1ZDT · UniProt Q13285 · UniProt Q15596

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