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MACA-H93G

Analyse MACA-H93G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AAO
Type: protein
Length: 608 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C551 peroxidase
EC: 1.11.1.5
UniProt: Q74FY6
Ligands: HEC, CA, SO4
Pockets: 3 · best druggability 0.88

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C551 peroxidase (EC 1.11.1.5)	protein	303	42% helix, 8% strand	Q74FY6
B	Cytochrome C551 peroxidase (EC 1.11.1.5)	protein	305	41% helix, 9% strand	Q74FY6

Ligands and binding sites

HEC · Heme C · ligand · 4 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 11 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	957	0.88	0.89	118	HEC, CA
2	1116	0.85	0.86	126	HEC, SO4
3	78	0.50	0.84	30	empty

Interfaces

1 interface between chains.

A–B · 1373 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 cofactor (heme c attachment).

Compared structures

4AAO · MacA-H93G · 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 Q74FY6
Elsewhere: RCSB PDB 4AAO · PDBe 4AAO · UniProt Q74FY6

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