2RD8 PDB NFT

Human Thymidylate Synthase Stabilized in Active Conformation by R163K Mutation: Asymmetry and Reactivity of Cys195

MOLNFT AF v1 smart contract in GenesisL1 blockchain:

0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba

IPFS of NFT metadata:

bafybeics3yl7qfwove5dtchu6xqbnjwf2ttozvst33abxvhzf4erochwg4/metadata.json

IPFS of structure file:

bafybeif2bvqnduufu2mpdtethwkwo5qltere7borcff6nevycyuzkqsu3y/2rd8.pdb

MOLNFT PDB v1

NFT id:
50266
PDB ID:
2RD8
Name:
Human Thymidylate Synthase Stabilized in Active Conformation by R163K Mutation: Asymmetry and Reactivity of Cys195
Keywords:
TRANSFERASE
Experimental Method:
X-RAY DIFFRACTION
Resolution:
2.50

NFT data

MolNFT PDB v1 is The Protein Data Bank database (URL: https://rcsb.org) of protein structures minted as ERC-721 NFT tokens on GenesisL1 blockchain for public free use, research and entertainment:

H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig, I.N. Shindyalov, P.E. Bourne.
(2000) The Protein Data Bank Nucleic Acids Research, 28: 235-242.

MOLNFT 2RD8 research and analysis (ICN3D with VR)

FASTA sequences

>2rd8_A mol:protein length:313 Thymidylate synthase
MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV
>2rd8_B mol:protein length:313 Thymidylate synthase
MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV

References and links

Current molecular structure file and data about current molecular structure file and NFT token based on it with
PDBID: 2RD8
TITLE: Human Thymidylate Synthase Stabilized in Active Conformation by R163K Mutation: Asymmetry and Reactivity of Cys195
DOI: 10.1021/bi7019386
AUTHORS: Gibson, L.M., Lovelace, L.L., Lebioda, L.
ACCESSION DATE: 09/21/07
Obtained at RCSB PDB https://rcsb.org
RCSB Link: https://www.rcsb.org/structure/2RD8