MolNFT v1 · #108743 · protein

Crystal structure of staphylococcus capitis divalent metal ion transporter (dmt) in complex with nanobody

4WGV · Divalent metal cation transporter mnth: “Crystal structure of staphylococcus capitis divalent metal ion transporter (dmt) in complex with nanobody”. X-ray diffraction, 20 pockets (best druggability 0.70). MolNFT v1 #108743 on…

PDB: 4WGV
Type: protein
Length: 1,030 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Divalent metal cation transporter mnth; Camelid antibody fragment, nanobody
UniProt: F9L8R0
Pockets: 20 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Divalent metal cation transporter mnth	protein	395	72% helix, 0% strand	F9L8R0
B, D	Camelid antibody fragment, nanobody	protein	120	3% helix, 57% strand	—

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	746	0.70	0.77	78	empty
2	67	0.68	0.95	26	empty
3	514	0.65	0.76	49	empty
4	136	0.64	0.86	22	empty
5	337	0.61	0.78	41	empty

Interfaces

4 interfaces between chains.

D–C · 842 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 828 Å² buried · 18 hydrogen bonds · protein-protein
A–C · 610 Å² buried · 0 hydrogen bonds · protein-protein
B–D · 503 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

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 F9L8R0
Elsewhere: RCSB PDB 4WGV · PDBe 4WGV · UniProt F9L8R0

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.