MolNFT v1 · #148964 · protein + DNA

The crystal structure of S. aureus gyrase complex with id-130 and DNA

6FM4: “The crystal structure of S. aureus gyrase complex with id-130 and DNA”. X-ray diffraction, 2 ligands (DU5, MN). MolNFT v1 #148964 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6FM4
Type: protein + DNA
Length: 1,381 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P66937, Q99XG5
Ligands: DU5, MN

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	—	protein	672	—	P66937, Q99XG5
D	—	protein	670	—	P66937, Q99XG5
E	—	dna	20	—	—
F	—	dna	19	—	—

Ligands and binding sites

DU5 · ~{N}-[3-(4-isoquinolin-1-ylpiperazin-1-yl) propyl]benzamide · ligand · chains B, D, E, F
MN · Manganese (II) ion · metal · 3 copies · chains B, E, D, F

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

Compared structures

6FM4 · The crystal structure of S. aureus Gyrase complex with ID-130 and DNA · the same entry in another collection · chain B against B, TM-score 1.00
Q99XG5 · AlphaFold monomer V2.0 prediction for DNA gyrase subunit a (Q99XG5) · a predicted model of the same protein · chain B against A, TM-score 0.72
P66937 · AlphaFold monomer V2.0 prediction for DNA gyrase subunit B (P66937) · a predicted model of the same protein · chain D against A, TM-score 0.28

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 P66937
Every structure of UniProt Q99XG5
Elsewhere: RCSB PDB 6FM4 · PDBe 6FM4 · UniProt P66937 · UniProt Q99XG5

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