MolNFT v1 · #21583 · protein

Crystal structure of the carboxy-terminal domain of htpg, the E. COLI HSP90

1SF8 · Chaperone protein htpg: “Crystal structure of the carboxy-terminal domain of htpg, the E. COLI HSP90”. X-ray diffraction, 2 ligands (NI, CL), 15 pockets (best druggability 0.77). MolNFT v1 #21583 on GenesisL1: 3D structure, binding…

PDB: 1SF8
Type: protein
Length: 932 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein htpg
UniProt: P0A6Z3
Ligands: NI, CL
Pockets: 15 · best druggability 0.77

Structure

x-ray diffraction · 4 distinct chains · 51% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E, F	Chaperone protein htpg	protein	115	53% helix, 10% strand	P0A6Z3
C	Chaperone protein htpg	protein	120	48% helix, 13% strand	P0A6Z3
G	Chaperone protein htpg	protein	121	51% helix, 10% strand	P0A6Z3
H	Chaperone protein htpg	protein	116	54% helix, 10% strand	P0A6Z3

Ligands and binding sites

NI · Nickel (II) ion · metal · 3 copies · chains C, D, G
CL · Chloride ion · ion · 3 copies · chains E, F, B, H

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

Pockets

15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	952	0.77	0.80	71	empty
2	870	0.70	0.75	66	empty
3	222	0.59	0.80	26	empty
4	189	0.57	0.80	26	empty
5	185	0.50	0.77	25	empty

Interfaces

15 interfaces between chains.

D–F · 946 Å² buried · 12 hydrogen bonds · protein-protein
A–G · 935 Å² buried · 8 hydrogen bonds · protein-protein
B–H · 933 Å² buried · 9 hydrogen bonds · protein-protein
C–E · 914 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 550 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 modified (engineered).

Compared structures

1SF8 · Crystal structure of the carboxy-terminal domain of htpG, the E. coli Hsp90 · the same entry in another collection · chain H against H, TM-score 1.00
P0A6Z3 · AlphaFold monomer V2.0 prediction for chaperone protein htpg (P0A6Z3) · a predicted model of the same protein · chain A 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 P0A6Z3
Elsewhere: RCSB PDB 1SF8 · PDBe 1SF8 · UniProt P0A6Z3

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