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Carbon regulatory pii-like protein sbtb from synechocystis sp. 6803 in apo state, trigonal crystal form

Analyse Carbon regulatory pii-like protein sbtb from synechocystis sp. 6803 in apo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5O3P
Type: protein
Length: 297 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Membrane-associated protein SLR1513
UniProt: P73954
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 32% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Membrane-associated protein SLR1513	protein	97	33% helix, 42% strand	P73954
B	Membrane-associated protein SLR1513	protein	101	32% helix, 42% strand	P73954
C	Membrane-associated protein SLR1513	protein	99	32% helix, 41% strand	P73954

Ligands and binding sites

1PE · Pentaethylene glycol · additive · 2 copies · chains A, B, C
PEG · Di(hydroxyethyl)ether · additive · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	230	0.68	0.85	37	empty
2	264	0.65	0.82	26	1PE
3	253	0.63	0.81	28	1PE
4	59	0.28	0.74	17	PEG

Interfaces

3 interfaces between chains.

A–C · 930 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 872 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 863 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

5O3P · Carbon regulatory PII-like protein SbtB from Synechocystis sp. 6803 in Apo state… · the same entry in another collection · chain A against A, TM-score 1.00
P73954 · AlphaFold monomer V2.0 prediction for membrane-associated protein SLR1513 (P73954) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P73954
Elsewhere: RCSB PDB 5O3P · PDBe 5O3P · UniProt P73954

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