MolNFT v1 · #27453 · protein

Divalent cation tolerant protein cuta from homo sapiens O60888

1XK8: “Divalent cation tolerant protein cuta from homo sapiens O60888”. X-ray diffraction, 1 ligand (NA), 12 pockets (best druggability 0.81). MolNFT v1 #27453 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1XK8
Type: protein
Length: 643 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Divalent cation tolerant protein cuta
UniProt: O60888
Ligands: NA
Pockets: 12 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, E, F	Divalent cation tolerant protein cuta	protein	107	34% helix, 41% strand	O60888
D	Divalent cation tolerant protein cuta	protein	108	33% helix, 39% strand	O60888

Ligands and binding sites

NA · Sodium ion · metal · 3 copies · chains A, B, E, F, C, D

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

Pockets

12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	448	0.81	0.88	52	NA
2	239	0.56	0.78	29	NA
3	133	0.55	0.81	20	empty
4	161	0.53	0.79	17	empty
5	126	0.53	0.81	17	empty

Interfaces

12 interfaces between chains.

D–E · 1226 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 1223 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 1207 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 1187 Å² buried · 14 hydrogen bonds · protein-protein
E–F · 1159 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

1XK8 · Divalent cation tolerant protein CUTA from Homo sapiens O60888 · the same entry in another collection · chain F against F, TM-score 1.00
O60888 · AlphaFold monomer V2.0 prediction for protein cuta (O60888) · a predicted model of the same protein · 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 O60888
Elsewhere: RCSB PDB 1XK8 · PDBe 1XK8 · UniProt O60888

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