MolNFT v1 · #146099 · protein

Complex structure of methane monooxygenase hydroxylase in complex with inhibitory subunit

6D7K · Methane monooxygenase hydroxylase, MMOX1: “Complex structure of methane monooxygenase hydroxylase in complex with inhibitory subunit”. X-ray diffraction, 1 ligand (FE), 20 pockets (best druggability 0.87). MolNFT v1 #146099 on…

PDB: 6D7K
Type: protein
Length: 2,148 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methane monooxygenase hydroxylase, MMOX1; Methane monooxygenase hydroxylase, mmoy…
UniProt: Q27RN7, Q27RN6, Q27RN4, Q27RN3
Ligands: FE
Pockets: 20 · best druggability 0.87

Structure

x-ray diffraction · 7 distinct chains · 61% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methane monooxygenase hydroxylase, MMOX1	protein	503	60% helix, 4% strand	Q27RN7
B, F	Methane monooxygenase hydroxylase, mmoy	protein	339	71% helix, 1% strand	Q27RN6
C	Methane monooxygenase hydroxylase, mmoz	protein	165	65% helix, 4% strand	Q27RN4
D	Methane monooxygenase hydroxylase, mmod	protein	64	33% helix, 44% strand	Q27RN3
E	Methane monooxygenase hydroxylase, MMOX1	protein	503	60% helix, 4% strand	Q27RN7
G	Methane monooxygenase hydroxylase, mmoz	protein	167	63% helix, 4% strand	Q27RN4
H	Methane monooxygenase hydroxylase, mmod	protein	68	29% helix, 40% strand	Q27RN3

Ligands and binding sites

FE · Fe (III) ion · metal · 4 copies · chains A, E
HEZ · Hexane-1,6-diol · additive · 2 copies · chains A, E
FMT · Formic acid · additive · 2 copies · chains A, E

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

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	389	0.87	0.96	56	HEZ, FMT
2	882	0.82	0.84	81	empty
3	175	0.81	0.96	35	HEZ, FMT
4	119	0.80	0.98	24	empty
5	143	0.80	0.97	27	empty

Interfaces

14 interfaces between chains.

E–F · 3949 Å² buried · 61 hydrogen bonds · protein-protein
A–B · 3884 Å² buried · 63 hydrogen bonds · protein-protein
E–G · 2177 Å² buried · 33 hydrogen bonds · protein-protein
A–C · 2016 Å² buried · 31 hydrogen bonds · protein-protein
B–F · 1685 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

6D7K · Complex structure of Methane monooxygenase hydroxylase in complex with inhibitory subunit · 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 Q27RN7
Every structure of UniProt Q27RN6
Every structure of UniProt Q27RN4
Every structure of UniProt Q27RN3
Elsewhere: RCSB PDB 6D7K · PDBe 6D7K · UniProt Q27RN7 · UniProt Q27RN6 · UniProt Q27RN4 · UniProt Q27RN3

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