MolNFT v1 · #134500 · protein

The hhoa protease from synechocystis sp. pcc 6803

5T63 · Putative serine protease hhoa: “The hhoa protease from synechocystis sp. pcc 6803”. X-ray diffraction, 1 ligand (MG), 1 pocket (best druggability 0.36). MolNFT v1 #134500 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5T63
Type: protein
Length: 287 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative serine protease hhoa; Ala-ala-ala-ala
UniProt: P72780
Ligands: MG
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 19% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative serine protease hhoa	protein	283	19% helix, 38% strand	P72780
C	Ala-ala-ala-ala	protein	4	0% helix, 50% strand	—

Ligands and binding sites

MG · Magnesium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	94	0.36	0.75	18	empty

Interfaces

1 interface between chains.

A–C · 277 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5T63 · The HhoA protease from Synechocystis sp. PCC 6803 · the same entry in another collection · chain A against A, TM-score 1.00
P72780 · AlphaFold monomer V2.0 prediction for putative serine protease hhoa (P72780) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P72780
Elsewhere: RCSB PDB 5T63 · PDBe 5T63 · UniProt P72780

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