MolNFT v1 · #187253 · protein

Complex structure of methane monooxygenase hydroxylase and regulatory subunit DBL2

7S6Q: “Complex structure of methane monooxygenase hydroxylase and regulatory subunit DBL2”. X-ray diffraction, 2 ligands (BEZ, FE). MolNFT v1 #187253 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7S6Q
Type: protein
Length: 2,410 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: A0A2D2D5X0, A0A2D2D5X7, A0A2D2D0T0, A0A2D2D0T8
Ligands: BEZ, FE

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E	—	protein	515	—	A0A2D2D5X0
B, F	—	protein	392	—	A0A2D2D5X7
C, G	—	protein	168	—	A0A2D2D0T0
D	—	protein	130	—	A0A2D2D0T8
H	—	protein	130	—	A0A2D2D0T8

Ligands and binding sites

BEZ · Benzoic acid · ligand · 2 copies · chains A, E
FE · Fe (III) ion · metal · 4 copies · chains A, E
EDO · 1,2-ethanediol · additive · 28 copies · chains A, D, B, H, C, E, F, G

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

Compared structures

7S6Q · Complex structure of Methane monooxygenase hydroxylase and regulatory subunit DBL2 · 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 A0A2D2D5X0
Every structure of UniProt A0A2D2D5X7
Every structure of UniProt A0A2D2D0T0
Every structure of UniProt A0A2D2D0T8
Elsewhere: RCSB PDB 7S6Q · PDBe 7S6Q · UniProt A0A2D2D5X0 · UniProt A0A2D2D5X7 · UniProt A0A2D2D0T0 · UniProt A0A2D2D0T8

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