MolNFT v1 · #165303 · protein + DNA + RNA

Rrn anti-termination complex without S4

6TQN · Inositol monophosphatase: “Rrn anti-termination complex without S4”. Electron microscopy, 2 ligands (MG, ZN), 20 pockets (best druggability 0.84). MolNFT v1 #165303 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6TQN
Type: protein + DNA + RNA
Length: 4,852 residues
Chains: 14
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
Ligands: MG, ZN
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 14 distinct chains · 34% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
T	Inositol monophosphatase	protein	255	39% helix, 25% strand	A0A5B7PBT3
S	Inositol-1-monophosphatase (EC 3.1.3.25)	protein	267	36% helix, 25% strand	P0ADG4
A	Transcription TERMINATION/ANTITERMINATION protein nusa	protein	495	35% helix, 12% strand	A0A4P8BVH6
B	Transcription antitermination protein nusb	protein	134	62% helix, 0% strand	A0A4P8C5Y7
E	30S ribosomal protein S10	protein	98	27% helix, 26% strand	A0A073G203
G	Transcription TERMINATION/ANTITERMINATION protein nusg	protein	178	24% helix, 19% strand	V0ZS55
U	DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6)	protein	322	24% helix, 25% strand	P0A7Z4
V	DNA-directed RNA polymerase subunit alpha (EC 2.7.7.6)	protein	222	22% helix, 34% strand	P0A7Z4
W	DNA-directed RNA polymerase subunit omega (EC 2.7.7.6)	protein	90	70% helix, 0% strand	P0A800
X	DNA-directed RNA polymerase subunit beta (EC 2.7.7.6)	protein	1342	30% helix, 19% strand	P0A8V4
Y	DNA-directed RNA polymerase subunit beta' (EC 2.7.7.6)	protein	1337	36% helix, 16% strand	S1HM87
R	Rrngnut	rna	45	—	—
L	Tdna	dna	34	—	—
K	Ntdna	dna	33	—	—

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	897	0.84	0.86	108	empty
2	1064	0.84	0.85	103	empty
3	683	0.83	0.88	70	empty
4	1161	0.82	0.83	89	empty
5	619	0.82	0.87	59	empty

Interfaces

40 interfaces between chains.

X–Y · 8278 Å² buried · 106 hydrogen bonds · protein-protein
U–V · 2331 Å² buried · 23 hydrogen bonds · protein-protein
U–X · 1902 Å² buried · 30 hydrogen bonds · protein-protein
T–S · 1610 Å² buried · 28 hydrogen bonds · protein-protein
A–R · 1505 Å² buried · 34 hydrogen bonds · protein-nucleic

Compared structures

6TQN · rrn anti-termination complex without S4 · 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
Elsewhere: RCSB PDB 6TQN · PDBe 6TQN · UniProt A0A5B7PBT3 · UniProt P0ADG4 · UniProt A0A4P8BVH6 · UniProt A0A4P8C5Y7 · UniProt A0A073G203 · UniProt V0ZS55 · UniProt P0A7Z4 · UniProt P0A800 · UniProt P0A8V4 · UniProt S1HM87

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