MolNFT v1 · #7781 · protein

Crystal structure of C-phycocyanin from spirulina platensis

1GH0 · C-phycocyanin alpha subunit: “Crystal structure of C-phycocyanin from spirulina platensis”. X-ray diffraction, 1 ligand (CYC), 20 pockets (best druggability 0.84). MolNFT v1 #7781 on GenesisL1: 3D structure, binding sites and…

PDB: 1GH0
Type: protein
Length: 4,008 residues
Chains: 24
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-phycocyanin alpha subunit; C-phycocyanin beta subunit
UniProt: P72509, P72508
Ligands: CYC
Pockets: 20 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G, I, K, M, O, Q, S, U, W	C-phycocyanin alpha subunit	protein	162	78% helix, 0% strand	P72509
B, D, F, H, J, L, N, P, R, T, V, X	C-phycocyanin beta subunit	protein	172	77% helix, 0% strand	P72508

Ligands and binding sites

CYC · Phycocyanobilin · ligand · 36 copies · chains A, D, B, K, C, F, I, E, G, J, H, L, U, M, P, N, W, O, R, Q, S, V, T, X

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	363	0.84	0.92	37	CYC
2	347	0.83	0.92	38	CYC
3	360	0.83	0.92	38	CYC
4	353	0.83	0.92	40	CYC
5	334	0.83	0.92	39	CYC

Interfaces

66 interfaces between chains.

C–D · 1629 Å² buried · 13 hydrogen bonds · protein-protein
K–L · 1622 Å² buried · 11 hydrogen bonds · protein-protein
Q–R · 1617 Å² buried · 13 hydrogen bonds · protein-protein
W–X · 1615 Å² buried · 10 hydrogen bonds · protein-protein
S–T · 1615 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 36 cofactor, 12 modified (phycocyanobilin attachment, nonstandard).

Compared structures

1GH0 · Crystal structure of C-phycocyanin from spirulina platensis · the same entry in another collection · chain K against K, 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 P72509
Every structure of UniProt P72508
Elsewhere: RCSB PDB 1GH0 · PDBe 1GH0 · UniProt P72509 · UniProt P72508

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