MolNFT v1 · #33234 · protein

Edta treated

2CE7 · Cell division protein ftsh: “Edta treated”. X-ray diffraction, 3 ligands (ADP, ZN, MG), 20 pockets (best druggability 0.79). MolNFT v1 #33234 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2CE7
Type: protein
Length: 2,468 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsh
UniProt: Q9WZ49
Ligands: ADP, ZN, MG
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 6 distinct chains · 58% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsh	protein	406	58% helix, 9% strand	Q9WZ49
B	Cell division protein ftsh	protein	411	58% helix, 9% strand	Q9WZ49
C	Cell division protein ftsh	protein	421	57% helix, 8% strand	Q9WZ49
D	Cell division protein ftsh	protein	413	58% helix, 9% strand	Q9WZ49
E	Cell division protein ftsh	protein	405	58% helix, 9% strand	Q9WZ49
F	Cell division protein ftsh	protein	412	58% helix, 9% strand	Q9WZ49

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
MG · Magnesium ion · metal · 6 copies · chains A, B, C, D, E, F

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

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	846	0.79	0.82	78	empty
2	805	0.76	0.80	83	ZN
3	58	0.74	0.98	19	empty
4	766	0.71	0.78	90	ADP
5	1191	0.69	0.74	105	ADP, MG

Interfaces

11 interfaces between chains.

D–E · 1808 Å² buried · 30 hydrogen bonds · protein-protein
A–B · 1792 Å² buried · 26 hydrogen bonds · protein-protein
B–C · 1696 Å² buried · 27 hydrogen bonds · protein-protein
E–F · 1337 Å² buried · 17 hydrogen bonds · protein-protein
A–E · 234 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2CE7 · EDTA treated · the same entry in another collection · chain F against F, TM-score 1.00
Q9WZ49 · AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh (Q9WZ49) · a predicted model of the same protein · chain B against A, TM-score 0.65

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 Q9WZ49
Elsewhere: RCSB PDB 2CE7 · PDBe 2CE7 · UniProt Q9WZ49

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