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Crystal structure of wild-type of E. COLI CUTA1

Analyse Crystal structure of wild-type of E. COLI CUTA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3X3U
Type: protein
Length: 624 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Divalent-cation tolerance protein cuta
UniProt: P69488
Pockets: 12 · best druggability 0.77

Structure

x-ray diffraction · 4 distinct chains · 35% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Divalent-cation tolerance protein cuta	protein	104	35% helix, 42% strand	P69488
B, F	Divalent-cation tolerance protein cuta	protein	104	35% helix, 42% strand	P69488
C	Divalent-cation tolerance protein cuta	protein	105	35% helix, 41% strand	P69488
E	Divalent-cation tolerance protein cuta	protein	103	35% helix, 42% strand	P69488

Pockets

12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	75	0.77	0.98	18	empty
2	77	0.77	0.97	18	empty
3	340	0.71	0.84	48	empty
4	233	0.62	0.81	37	empty
5	84	0.57	0.86	15	empty

Interfaces

12 interfaces between chains.

A–C · 1123 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 1122 Å² buried · 17 hydrogen bonds · protein-protein
D–F · 1107 Å² buried · 14 hydrogen bonds · protein-protein
D–E · 1106 Å² buried · 14 hydrogen bonds · protein-protein
E–F · 1097 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3X3U · Crystal structure of wild-type of E. coli CutA1 · the same entry in another collection · chain F against F, TM-score 1.00
P69488 · AlphaFold monomer V2.0 prediction for divalent-cation tolerance protein cuta (P69488) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 P69488
Elsewhere: RCSB PDB 3X3U · PDBe 3X3U · UniProt P69488

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