Research workbench

Mycobacterium tuberculosis rnap HOLO/RBPA in relaxed state

Analyse Mycobacterium tuberculosis rnap HOLO/RBPA in relaxed state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6C05
Type: protein
Length: 3,353 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: A0A045J8T1, V9Z879, A0A045J9E2, A0A0T9N9K3, A0A045HD00, A0A045IP01
Ligands: ZN, MG

Structure

electron microscopy · 7 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	226	—	A0A045J8T1
B	—	protein	237	—	A0A045J8T1
C	—	protein	1111	—	V9Z879
D	—	protein	1263	—	A0A045J9E2
E	—	protein	83	—	A0A0T9N9K3
F	—	protein	326	—	A0A045HD00
J	—	protein	107	—	A0A045IP01

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains D
MG · Magnesium ion · metal · chains D

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

Compared structures

6C05 · Mycobacterium tuberculosis RNAP Holo/RbpA in relaxed state · 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 A0A045J8T1
Every structure of UniProt V9Z879
Every structure of UniProt A0A045J9E2
Every structure of UniProt A0A0T9N9K3
Every structure of UniProt A0A045HD00
Every structure of UniProt A0A045IP01
Elsewhere: RCSB PDB 6C05 · PDBe 6C05 · UniProt A0A045J8T1 · UniProt V9Z879 · UniProt A0A045J9E2 · UniProt A0A0T9N9K3 · UniProt A0A045HD00 · UniProt A0A045IP01

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