Research workbench

Microcin C7 self immunity protein mccf in complex aspartyl sulfamoyl adenosine

Analyse Microcin C7 self immunity protein mccf in complex aspartyl sulfamoyl adenosine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TLB
Type: protein
Length: 670 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mccf
UniProt: Q2KKH9
Ligands: DSZ
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Mccf	protein	335	31% helix, 23% strand	Q2KKH9

Ligands and binding sites

DSZ · 5'-O-(L-alpha-aspartylsulfamoyl)adenosine · ligand · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	659	0.68	0.77	79	DSZ
2	158	0.53	0.80	24	empty
3	86	0.52	0.84	19	empty
4	57	0.32	0.76	11	empty
5	50	0.30	0.76	11	empty

Interfaces

1 interface between chains.

A–B · 1884 Å² buried · 49 hydrogen bonds · protein-protein

Compared structures

3TLB · Microcin C7 self immunity protein MccF in complex aspartyl sulfamoyl adenosine · the same entry in another collection · chain B against B, 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 Q2KKH9
Elsewhere: RCSB PDB 3TLB · PDBe 3TLB · UniProt Q2KKH9

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