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CO2 concentrating mechanism protein P, ccmp form 1

Analyse CO2 concentrating mechanism protein P, ccmp form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HT5
Type: protein
Length: 1,219 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CO2 concentrating mechanism protein P
UniProt: Q5N3D0
Pockets: 9 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CO2 concentrating mechanism protein P	protein	204	41% helix, 30% strand	Q5N3D0
B, C, D, E, F	CO2 concentrating mechanism protein P	protein	203	41% helix, 30% strand	Q5N3D0

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1022	0.76	0.78	102	empty
2	582	0.69	0.77	62	empty
3	327	0.60	0.77	37	empty
4	209	0.45	0.73	30	empty
5	179	0.43	0.74	30	empty

Interfaces

15 interfaces between chains.

A–D · 1243 Å² buried · 23 hydrogen bonds · protein-protein
B–E · 1165 Å² buried · 17 hydrogen bonds · protein-protein
C–F · 1132 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 1003 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 1000 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

4HT5 · CO2 concentrating mechanism protein P, CcmP form 1 · 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 4HT5 · PDBe 4HT5 · UniProt Q5N3D0

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