MolNFT v1 · #167143 · protein

Cinnamate 4-hydroxylase (C4H1) from sorghum bicolor

6VBY: “Cinnamate 4-hydroxylase (C4H1) from sorghum bicolor”. X-ray diffraction, 1 ligand (HEM). MolNFT v1 #167143 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6VBY
Type: protein
Length: 470 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q94IP1
Ligands: HEM

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	470	—	Q94IP1

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
GOL · Glycerol · additive · 2 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Compared structures

6VBY · Cinnamate 4-hydroxylase (C4H1) from Sorghum bicolor · the same entry in another collection · chain A against A, TM-score 1.00
Q94IP1 · AlphaFold monomer V2.0 prediction for trans-cinnamate 4-monooxygenase (Q94IP1) · 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 Q94IP1
Elsewhere: RCSB PDB 6VBY · PDBe 6VBY · UniProt Q94IP1

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