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Crystal structure of chlamydomonas reinhardtii THB4

Analyse Crystal structure of chlamydomonas reinhardtii THB4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BME
Type: protein
Length: 252 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Truncated hemoglobin 4
UniProt: R9RY64
Ligands: HEM, SO4
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Truncated hemoglobin 4	protein	127	72% helix, 0% strand	R9RY64
B	Truncated hemoglobin 4	protein	125	73% helix, 0% strand	R9RY64

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

3 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	654	0.75	0.81	64	HEM, SO4
2	227	0.70	0.85	28	HEM
3	50	0.28	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 540 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6BME · Crystal structure of Chlamydomonas reinhardtii THB4 · 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 R9RY64
Elsewhere: RCSB PDB 6BME · PDBe 6BME · UniProt R9RY64

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