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CSR/RSM protein-RNA recognition - a molecular affinity ruler: RSMZ(SL4)/RSME(DIMER) 2:1 complex

Analyse CSR/RSM protein-RNA recognition - a molecular affinity ruler… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MFG
Type: protein + RNA
Length: 160 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbon storage regulator homolog; SL4(RSMZ) RNA
UniProt: Q5MXB2
Pockets: 1 · best druggability 0.39

Structure

solution nmr · 2 distinct chains · 8% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Carbon storage regulator homolog	protein	59	8% helix, 49% strand	Q5MXB2
B, D	SL4(RSMZ) RNA	rna	21	—	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	154	0.39	0.73	29	empty

Interfaces

5 interfaces between chains.

A–C · 2047 Å² buried · 35 hydrogen bonds · protein-protein
B–C · 642 Å² buried · 15 hydrogen bonds · protein-nucleic
A–D · 572 Å² buried · 14 hydrogen bonds · protein-nucleic
C–D · 449 Å² buried · 12 hydrogen bonds · protein-nucleic
A–B · 435 Å² buried · 12 hydrogen bonds · protein-nucleic

Compared structures

2MFG · Csr/Rsm protein-RNA recognition - A molecular affinity ruler: RsmZ(SL4)/RsmE(dimer) 2:1… · 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 Q5MXB2
Elsewhere: RCSB PDB 2MFG · PDBe 2MFG · UniProt Q5MXB2

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