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Complex structure of methane monooxygenase hydroxylase and regulatory subunit DBL2

Analyse Complex structure of methane monooxygenase hydroxylase and regulatory subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7S7H
Type: protein
Length: 2,410 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methane monooxygenase component a alpha chain; Methane monooxygenase beta chain; Methane…
EC: 1.-.-.-
UniProt: A0A2D2D5X0, A0A2D2D5X7, A0A2D2D0T0, A0A2D2D0T8
Ligands: FE
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 6 distinct chains · 59% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E	Methane monooxygenase component a alpha chain (EC 1.-.-.-)	protein	515	62% helix, 4% strand	A0A2D2D5X0
B, F	Methane monooxygenase beta chain	protein	392	66% helix, 1% strand	A0A2D2D5X7
C	Methane monooxygenase gamma chain	protein	167	63% helix, 4% strand	A0A2D2D0T0
D	Methane monooxygenase regulatory protein B	protein	131	38% helix, 30% strand	A0A2D2D0T8
G	Methane monooxygenase gamma chain	protein	168	63% helix, 4% strand	A0A2D2D0T0
H	Methane monooxygenase regulatory protein B	protein	130	36% helix, 30% strand	A0A2D2D0T8

Ligands and binding sites

FE · Fe (III) ion · metal · 4 copies · chains A, E
EDO · 1,2-ethanediol · additive · 18 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.

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1169	0.86	0.87	122	EDO
2	113	0.79	0.98	35	empty
3	102	0.79	0.99	34	empty
4	94	0.78	0.98	23	empty
5	86	0.77	0.98	23	empty

Interfaces

18 interfaces between chains.

A–B · 5381 Å² buried · 97 hydrogen bonds · protein-protein
E–F · 5358 Å² buried · 92 hydrogen bonds · protein-protein
A–D · 2657 Å² buried · 41 hydrogen bonds · protein-protein
E–H · 2649 Å² buried · 37 hydrogen bonds · protein-protein
E–G · 2235 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

7S7H · 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 7S7H · PDBe 7S7H · UniProt A0A2D2D5X0 · UniProt A0A2D2D5X7 · UniProt A0A2D2D0T0 · UniProt A0A2D2D0T8

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