MolNFT v1 · #178771 · protein

Heme binding to srrb pas domain plays a role in redox regulation of S. aureus srrab two-component system

7JL6 · Sensor protein srrb: “Heme binding to srrb pas domain plays a role in redox regulation of S. aureus srrab two-component system”. X-ray diffraction, 3 pockets (best druggability 0.47). MolNFT v1 #178771 on GenesisL1: 3D structure…

PDB: 7JL6
Type: protein
Length: 194 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sensor protein srrb
EC: 2.7.13.3
UniProt: Q9L523
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sensor protein srrb (EC 2.7.13.3)	protein	104	28% helix, 34% strand	Q9L523
B	Sensor protein srrb (EC 2.7.13.3)	protein	90	28% helix, 39% strand	Q9L523

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.47	0.83	13	empty
2	52	0.39	0.81	12	empty
3	60	0.32	0.75	11	empty

Interfaces

1 interface between chains.

A–B · 1025 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7JL6 · Heme binding to SrrB PAS domain plays a role in redox regulation of S. aureus SrrAB… · the same entry in another collection · chain A against A, TM-score 1.00
Q9L523 · AlphaFold monomer V2.0 prediction for sensor protein srrb (Q9L523) · a predicted model of the same protein · chain B against A, TM-score 0.91

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 Q9L523
Elsewhere: RCSB PDB 7JL6 · PDBe 7JL6 · UniProt Q9L523

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