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The structure of cca-adding enzyme apo form I

Analyse The structure of cca-adding enzyme apo form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3H37
Type: protein
Length: 836 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRNA nucleotidyl transferase-related protein
EC: 2.7.7.25
UniProt: Q9WZH4
Pockets: 6 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TRNA nucleotidyl transferase-related protein (EC 2.7.7.25)	protein	415	57% helix, 9% strand	Q9WZH4
B	TRNA nucleotidyl transferase-related protein (EC 2.7.7.25)	protein	421	55% helix, 10% strand	Q9WZH4

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	403	0.63	0.77	27	empty
2	153	0.51	0.78	26	empty
3	69	0.46	0.83	15	empty
4	215	0.43	0.73	36	empty
5	52	0.36	0.79	12	empty

Interfaces

1 interface between chains.

A–B · 677 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 19 modified (engineered).

Compared structures

3H37 · The structure of CCA-adding enzyme apo form I · 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 Q9WZH4
Elsewhere: RCSB PDB 3H37 · PDBe 3H37 · UniProt Q9WZH4

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