MolNFT v1 · #121003 · protein

Structure of T-type phycobiliprotein lyase cpet from prochlorococcus phage P-HM1

5HI8 · Antenna protein: “Structure of T-type phycobiliprotein lyase cpet from prochlorococcus phage P-HM1”. X-ray diffraction, 1 ligand (MG), 1 pocket (best druggability 0.84). MolNFT v1 #121003 on GenesisL1: 3D structure, binding sites…

PDB: 5HI8
Type: protein
Length: 272 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Antenna protein
UniProt: E3SMK9
Ligands: MG
Pockets: 1 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Antenna protein	protein	136	11% helix, 51% strand	E3SMK9

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
ACT · Acetate ion · additive · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	888	0.84	0.86	100	ACT

Interfaces

1 interface between chains.

A–B · 667 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

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 E3SMK9
Elsewhere: RCSB PDB 5HI8 · PDBe 5HI8 · UniProt E3SMK9

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