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Crystal structures of the first condensation domain of the cda synthetase

Analyse Crystal structures of the first condensation domain of the cda synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JN5
Type: protein
Length: 860 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cda peptide synthetase I
UniProt: Q9Z4X6
Pockets: 7 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cda peptide synthetase I	protein	435	38% helix, 22% strand	Q9Z4X6
B	Cda peptide synthetase I	protein	425	39% helix, 23% strand	Q9Z4X6

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	614	0.85	0.90	82	empty
2	493	0.82	0.89	64	empty
3	296	0.61	0.79	47	empty
4	88	0.50	0.83	23	empty
5	64	0.36	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 850 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4JN5 · Crystal structures of the first condensation domain of the CDA synthetase · 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 Q9Z4X6
Elsewhere: RCSB PDB 4JN5 · PDBe 4JN5 · UniProt Q9Z4X6

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