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BCS1 aaa domain

Analyse BCS1 aaa domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6U1Y
Type: protein
Length: 1,709 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitochondrial chaperone BCS1
UniProt: Q9CZP5
Ligands: ANP, MG
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 5 distinct chains · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D, F	Mitochondrial chaperone BCS1	protein	244	43% helix, 16% strand	Q9CZP5
B	Mitochondrial chaperone BCS1	protein	245	44% helix, 16% strand	Q9CZP5
C	Mitochondrial chaperone BCS1	protein	242	43% helix, 16% strand	Q9CZP5
E	Mitochondrial chaperone BCS1	protein	246	43% helix, 16% strand	Q9CZP5
G	Mitochondrial chaperone BCS1	protein	244	43% helix, 16% strand	Q9CZP5

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 7 copies · chains A, G, B, E, C, D, F
MG · Magnesium ion · metal · 7 copies · chains A, G, B, E, C, D, F

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	471	0.81	0.88	73	ANP, MG
2	522	0.81	0.87	75	ANP, MG
3	453	0.80	0.88	69	ANP, MG
4	411	0.80	0.89	57	ANP, MG
5	509	0.80	0.87	76	ANP, MG

Interfaces

7 interfaces between chains.

D–F · 1580 Å² buried · 12 hydrogen bonds · protein-protein
A–D · 1561 Å² buried · 11 hydrogen bonds · protein-protein
A–G · 1545 Å² buried · 10 hydrogen bonds · protein-protein
E–F · 1541 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 1532 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

6U1Y · bcs1 AAA domain · the same entry in another collection · chain G against G, TM-score 1.00
Q9CZP5 · AlphaFold monomer V2.0 prediction for mitochondrial chaperone BCS1 (Q9CZP5) · a predicted model of the same protein · chain C 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 Q9CZP5
Elsewhere: RCSB PDB 6U1Y · PDBe 6U1Y · UniProt Q9CZP5

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