MolNFT v1 · #27308 · protein

Crystal structure of anthrax edema factor (ef) truncation mutant, ef- delta 64 in complex with calmodulin

1XFU · Calmodulin-sensitive adenylate cyclase: “Crystal structure of anthrax edema factor (ef) truncation mutant, ef- delta 64 in complex with calmodulin”. X-ray diffraction, 2 ligands (CA, MG), 20 pockets (best druggability 0.74). MolNFT…

PDB: 1XFU
Type: protein
Length: 5,286 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin-sensitive adenylate cyclase; Calmodulin 2
EC: 4.6.1.1
UniProt: P40136, P62158
Ligands: CA, MG
Pockets: 20 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1)	protein	735	38% helix, 12% strand	P40136
O, P, Q, R, S, T	Calmodulin 2	protein	146	48% helix, 5% strand	P62158

Ligands and binding sites

CA · Calcium ion · metal · 18 copies · chains O, P, Q, R, S, T
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, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	935	0.74	0.78	79	empty
2	887	0.74	0.78	76	empty
3	952	0.73	0.77	87	empty
4	865	0.73	0.78	65	empty
5	791	0.73	0.78	70	empty

Interfaces

12 interfaces between chains.

F–T · 2990 Å² buried · 21 hydrogen bonds · protein-protein
A–O · 2986 Å² buried · 22 hydrogen bonds · protein-protein
D–R · 2983 Å² buried · 22 hydrogen bonds · protein-protein
C–Q · 2982 Å² buried · 21 hydrogen bonds · protein-protein
B–P · 2982 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

1XFU · Crystal structure of anthrax edema factor (EF) truncation mutant, EF-delta 64 in complex… · the same entry in another collection · chain T against T, 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 P40136
Every structure of UniProt P62158
Elsewhere: RCSB PDB 1XFU · PDBe 1XFU · UniProt P40136 · UniProt P62158

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