MolNFT v1 · #149328 · protein

Dimerization domain of TP901-1 ci repressor

6FXA: “Dimerization domain of TP901-1 ci repressor”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.85). MolNFT v1 #149328 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6FXA
Type: protein
Length: 209 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ci
UniProt: O48503
Ligands: SO4
Pockets: 1 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, E, F	Ci	protein	35	80% helix, 0% strand	O48503
D	Ci	protein	34	82% helix, 0% strand	O48503

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, C

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	243	0.85	0.97	33	empty

Interfaces

13 interfaces between chains.

E–F · 1443 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 1383 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 1360 Å² buried · 21 hydrogen bonds · protein-protein
B–E · 661 Å² buried · 5 hydrogen bonds · protein-protein
D–F · 569 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6FXA · Dimerization domain of TP901-1 CI repressor · 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 O48503
Elsewhere: RCSB PDB 6FXA · PDBe 6FXA · UniProt O48503

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