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CO2 concentrating mechanism protein P, ccmp form 2

Analyse CO2 concentrating mechanism protein P, ccmp form 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HT7
Type: protein
Length: 2,436 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CO2 concentrating mechanism protein P
UniProt: Q5N3D0
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, G, H, I, D, E, F, J, K, L	CO2 concentrating mechanism protein P	protein	203	39% helix, 30% strand	Q5N3D0

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1031	0.80	0.82	92	empty
2	1183	0.76	0.78	106	empty
3	833	0.74	0.79	70	empty
4	761	0.74	0.79	72	empty
5	800	0.73	0.78	74	empty

Interfaces

34 interfaces between chains.

C–F · 1153 Å² buried · 19 hydrogen bonds · protein-protein
I–L · 1150 Å² buried · 18 hydrogen bonds · protein-protein
B–E · 1149 Å² buried · 17 hydrogen bonds · protein-protein
A–D · 1147 Å² buried · 18 hydrogen bonds · protein-protein
H–K · 1147 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4HT7 · CO2 concentrating mechanism protein P, CcmP form 2 · 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 Q5N3D0
Elsewhere: RCSB PDB 4HT7 · PDBe 4HT7 · UniProt Q5N3D0

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