MolNFT v1 · #171265 · protein

ASPARTYL/ASPARAGINYL beta-hydroxylase (asph) oxygenase and tpr domains in complex with manganese, 4,4-dimethyl-2-oxoglutarate, and factor X substrate peptide FRAGMENT(39MER-4SER)

6YYY: “ASPARTYL/ASPARAGINYL beta-hydroxylase (asph) oxygenase and tpr domains in complex with manganese…”. X-ray diffraction, 2 ligands (Q1W, MN). MolNFT v1 #171265 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6YYY
Type: protein
Length: 446 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q12797, P00742
Ligands: Q1W, MN

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	428	—	Q12797
B	—	protein	18	—	P00742

Ligands and binding sites

Q1W · 2,2-dimethyl-4-oxidanylidene-pentanedioic acid · ligand · chains A
MN · Manganese (II) ion · metal · chains A

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

Compared structures

6YYY · Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
Q12797 · AlphaFold monomer V2.0 prediction for ASPARTYL/ASPARAGINYL beta- hydroxylase (Q12797) · a predicted model of the same protein · chain A against A, TM-score 0.99
P00742 · AlphaFold monomer V2.0 prediction for coagulation factor X (P00742) · a predicted model of the same protein · chain B against A, TM-score 0.23

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 Q12797
Every structure of UniProt P00742
Elsewhere: RCSB PDB 6YYY · PDBe 6YYY · UniProt Q12797 · UniProt P00742

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