Research workbench

Rrn anti-termination complex

Analyse Rrn anti-termination complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TQO
Type: protein + DNA + RNA
Length: 5,056 residues
Chains: 15
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inositol monophosphatase; Inositol-1-monophosphatase; Transcription…
EC: 3.1.3.25, 2.7.7.6
UniProt: A0A5B7PBT3, P0ADG4, A0A4P8BVH6, A0A4P8C5Y7, A0A073G203, V0ZS55, P0A7Z4, P0A800, P0A8V4, S1HM87, I2X692
Ligands: MG, ZN
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 15 distinct chains · 34% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
T	Inositol monophosphatase	protein	255	40% helix, 22% strand	A0A5B7PBT3
S	Inositol-1-monophosphatase (EC 3.1.3.25)	protein	267	35% helix, 27% strand	P0ADG4
A	Transcription TERMINATION/ANTITERMINATION protein nusa	protein	495	39% helix, 11% strand	A0A4P8BVH6
B	Transcription antitermination protein nusb	protein	134	63% helix, 0% strand	A0A4P8C5Y7
E	30S ribosomal protein S10	protein	98	26% helix, 29% strand	A0A073G203
G	Transcription TERMINATION/ANTITERMINATION protein nusg	protein	178	25% helix, 26% strand	V0ZS55
U	DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6)	protein	322	25% helix, 23% strand	P0A7Z4
V	DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6)	protein	222	23% helix, 30% strand	P0A7Z4
W	DNA-directed RNA polymerase subunit omega (EC 2.7.7.6)	protein	90	69% helix, 0% strand	P0A800
X	DNA-directed RNA polymerase subunit beta (EC 2.7.7.6)	protein	1342	30% helix, 20% strand	P0A8V4
Y	DNA-directed RNA polymerase subunit beta' (EC 2.7.7.6)	protein	1337	36% helix, 16% strand	S1HM87
C	30S ribosomal protein S4	protein	205	40% helix, 7% strand	I2X692
R	Rrngnut RNA	rna	45	—	—
L	Tdna	dna	34	—	—
K	Ntdna	dna	32	—	—

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains T, S, Y, R
ZN · Zinc ion · metal · 2 copies · chains Y

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1064	0.85	0.86	103	empty
2	700	0.84	0.88	68	empty
3	489	0.82	0.89	54	empty
4	593	0.81	0.87	58	empty
5	767	0.80	0.84	64	empty

Interfaces

43 interfaces between chains.

X–Y · 8594 Å² buried · 109 hydrogen bonds · protein-protein
U–V · 2321 Å² buried · 10 hydrogen bonds · protein-protein
U–X · 1839 Å² buried · 19 hydrogen bonds · protein-protein
T–S · 1596 Å² buried · 26 hydrogen bonds · protein-protein
A–R · 1387 Å² buried · 33 hydrogen bonds · protein-nucleic

Compared structures

6TQO · rrn anti-termination complex · the same entry in another collection · chain K against K, 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 A0A5B7PBT3
Every structure of UniProt P0ADG4
Every structure of UniProt A0A4P8BVH6
Every structure of UniProt A0A4P8C5Y7
Every structure of UniProt A0A073G203
Every structure of UniProt V0ZS55
Every structure of UniProt P0A7Z4
Every structure of UniProt P0A800
Every structure of UniProt P0A8V4
Every structure of UniProt S1HM87
Every structure of UniProt I2X692
Elsewhere: RCSB PDB 6TQO · PDBe 6TQO · UniProt A0A5B7PBT3 · UniProt P0ADG4 · UniProt A0A4P8BVH6 · UniProt A0A4P8C5Y7 · UniProt A0A073G203 · UniProt V0ZS55 · UniProt P0A7Z4 · UniProt P0A800 · UniProt P0A8V4 · UniProt S1HM87 · UniProt I2X692

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