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Trichodesmium TERY_3377 (idia) (futa) with iron and water ligands.

Analyse Trichodesmium TERY_3377 (idia) (futa) with iron and water ligands. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6G7P
Type: protein
Length: 636 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Extracellular solute-binding protein, family 1
UniProt: Q10Z45
Ligands: FE, CL
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Extracellular solute-binding protein, family 1	protein	318	47% helix, 18% strand	Q10Z45

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains B, A
CL · Chloride ion · ion · 2 copies · chains B, A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	549	0.67	0.77	65	empty
2	244	0.62	0.81	33	CL
3	137	0.40	0.74	23	FE
4	89	0.36	0.76	18	empty

Interfaces

1 interface between chains.

B–A · 808 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

6G7P · Trichodesmium Tery_3377 (IdiA) (FutA) with iron and water ligands. · 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 Q10Z45
Elsewhere: RCSB PDB 6G7P · PDBe 6G7P · UniProt Q10Z45

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