MolNFT v1 · #151337 · protein

Crystal structure of human SDS22

6HKW · Protein phosphatase 1 regulatory subunit 7: “Crystal structure of human SDS22”. X-ray diffraction, 1 ligand (SO4), 13 pockets (best druggability 0.76). MolNFT v1 #151337 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HKW
Type: protein
Length: 1,530 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein phosphatase 1 regulatory subunit 7
UniProt: Q15435
Ligands: SO4
Pockets: 13 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Protein phosphatase 1 regulatory subunit 7	protein	306	9% helix, 14% strand	Q15435

Ligands and binding sites

SO4 · Sulfate ion · ion · 20 copies · chains A, C, B, D, E

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

Pockets

13 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	923	0.76	0.79	69	empty
2	224	0.52	0.77	36	empty
3	182	0.50	0.78	37	empty
4	97	0.47	0.81	30	empty
5	73	0.34	0.76	21	empty

Interfaces

7 interfaces between chains.

B–D · 1639 Å² buried · 26 hydrogen bonds · protein-protein
A–C · 1623 Å² buried · 21 hydrogen bonds · protein-protein
A–D · 460 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 447 Å² buried · 3 hydrogen bonds · protein-protein
D–E · 320 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6HKW · Crystal structure of human SDS22 · the same entry in another collection · chain A against A, TM-score 1.00
Q15435 · AlphaFold monomer V2.0 prediction for protein phosphatase 1 regulatory subunit 7 (Q15435) · 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 Q15435
Elsewhere: RCSB PDB 6HKW · PDBe 6HKW · UniProt Q15435

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