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Crystal structure of a transition-metal-ion-binding betagamma- crystallin from methanosaeta thermophila

Analyse Crystal structure of a transition-metal-ion-binding betagamma- crystallin from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HT7
Type: protein
Length: 246 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: A0B567
Ligands: FE2
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Uncharacterized protein	protein	82	9% helix, 46% strand	A0B567

Ligands and binding sites

FE2 · Fe (II) ion · metal · chains A, B, C

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

Pockets

2 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	158	0.60	0.83	33	empty
2	289	0.58	0.77	38	empty

Interfaces

3 interfaces between chains.

A–C · 435 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 411 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 410 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

5HT7 · Crystal structure of a transition-metal-ion-binding betagamma-crystallin from… · 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 A0B567
Elsewhere: RCSB PDB 5HT7 · PDBe 5HT7 · UniProt A0B567

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