MolNFT v1 · #113816 · protein

Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues

5AQR · Heat shock cognate 71 kda protein: “Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues”. X-ray diffraction, 2 ligands (N8Y, CL), 14 pockets (best druggability 0.74). MolNFT v1 #113816…

PDB: 5AQR
Type: protein
Length: 1,480 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock cognate 71 kda protein; Bag family molecular chaperone regulator 1
EC: 3.6.3.51
UniProt: P11142, Q99933
Ligands: N8Y, CL
Pockets: 14 · best druggability 0.74

Structure

x-ray diffraction · 4 distinct chains · 57% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E	Heat shock cognate 71 kda protein (EC 3.6.3.51)	protein	381	39% helix, 30% strand	P11142
B	Bag family molecular chaperone regulator 1	protein	112	78% helix, 0% strand	Q99933
D	Bag family molecular chaperone regulator 1	protein	112	78% helix, 0% strand	Q99933
F	Bag family molecular chaperone regulator 1	protein	113	77% helix, 0% strand	Q99933

Ligands and binding sites

N8Y · 6-methoxyquinazolin-4-amine · ligand · 3 copies · chains A, C, E
CL · Chloride ion · ion · chains C
GOL · Glycerol · additive · 18 copies · chains A, B, C, D, E, F
DMS · Dimethyl sulfoxide · additive · 7 copies · chains A, B, C, E
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 3 copies · chains A, C, E

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

Pockets

14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	907	0.74	0.78	87	TRS, N8Y, DMS
2	1101	0.73	0.76	93	GOL
3	885	0.72	0.77	76	TRS, N8Y, DMS
4	98	0.71	0.94	33	TRS, DMS
5	693	0.64	0.74	53	N8Y

Interfaces

9 interfaces between chains.

E–F · 1050 Å² buried · 23 hydrogen bonds · protein-protein
A–B · 1044 Å² buried · 26 hydrogen bonds · protein-protein
C–D · 1030 Å² buried · 22 hydrogen bonds · protein-protein
C–F · 286 Å² buried · 3 hydrogen bonds · protein-protein
D–F · 160 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

Q99933 · AlphaFold monomer V2.0 prediction for bag family molecular chaperone regulator 1 (Q99933) · a predicted model of the same protein · chain B against A, TM-score 0.93
P11142 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P11142) · a predicted model of the same protein · chain A against A, TM-score 0.83

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 P11142
Every structure of UniProt Q99933
Elsewhere: RCSB PDB 5AQR · PDBe 5AQR · UniProt P11142 · UniProt Q99933

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