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Human steroidogenic acute regulatory protein

Analyse Human steroidogenic acute regulatory protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P0L
Type: protein
Length: 808 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Steroidogenic acute regulatory protein, mitochondrial
UniProt: P49675
Pockets: 15 · best druggability 0.79

Structure

x-ray diffraction · 4 distinct chains · 27% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Steroidogenic acute regulatory protein, mitochondrial	protein	210	27% helix, 36% strand	P49675
B	Steroidogenic acute regulatory protein, mitochondrial	protein	208	27% helix, 36% strand	P49675
C	Steroidogenic acute regulatory protein, mitochondrial	protein	205	28% helix, 36% strand	P49675
D	Steroidogenic acute regulatory protein, mitochondrial	protein	185	25% helix, 38% strand	P49675

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	305	0.79	0.90	39	empty
2	298	0.79	0.90	37	empty
3	294	0.77	0.89	36	empty
4	249	0.71	0.86	37	empty
5	488	0.69	0.79	59	empty

Interfaces

4 interfaces between chains.

A–B · 394 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 305 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 291 Å² buried · 1 hydrogen bond · protein-protein
A–D · 236 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3P0L · Human steroidogenic acute regulatory protein · the same entry in another collection · chain D against D, TM-score 1.00
P49675 · AlphaFold monomer V2.0 prediction for steroidogenic acute regulatory protein… · a predicted model of the same protein · chain C against A, TM-score 0.98

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 P49675
Elsewhere: RCSB PDB 3P0L · PDBe 3P0L · UniProt P49675

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