MolNFT v1 · #111250 · protein

Crystal structure of A102D mutant of HSP14.1 from sulfolobus solfatataricus P2

4YLB · Heat shock protein HSP20: “Crystal structure of A102D mutant of HSP14.1 from sulfolobus solfatataricus P2”. X-ray diffraction, 1 ligand (CL), 5 pockets (best druggability 0.63). MolNFT v1 #111250 on GenesisL1: 3D structure, binding…

PDB: 4YLB
Type: protein
Length: 491 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock protein HSP20
UniProt: D0KNS6
Ligands: CL
Pockets: 5 · best druggability 0.63

Structure

x-ray diffraction · 4 distinct chains · 15% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat shock protein HSP20	protein	128	19% helix, 41% strand	D0KNS6
B	Heat shock protein HSP20	protein	117	14% helix, 43% strand	D0KNS6
C	Heat shock protein HSP20	protein	127	13% helix, 40% strand	D0KNS6
D	Heat shock protein HSP20	protein	119	15% helix, 39% strand	D0KNS6

Ligands and binding sites

CL · Chloride ion · ion · 3 copies · chains A, B, D

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	522	0.63	0.76	58	empty
2	76	0.55	0.86	27	empty
3	65	0.30	0.74	17	empty
4	74	0.28	0.72	19	empty
5	54	0.26	0.74	19	empty

Interfaces

5 interfaces between chains.

C–D · 1974 Å² buried · 40 hydrogen bonds · protein-protein
A–B · 1965 Å² buried · 42 hydrogen bonds · protein-protein
A–C · 942 Å² buried · 14 hydrogen bonds · protein-protein
A–D · 370 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 367 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4YLB · Crystal Structure of A102D mutant of hsp14.1 from Sulfolobus solfatataricus P2 · the same entry in another collection · chain A against A, TM-score 1.00

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 D0KNS6
Elsewhere: RCSB PDB 4YLB · PDBe 4YLB · UniProt D0KNS6

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