1DRB PDB NFT

CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL CHANGES AND COOPERATIVITY IN BINDING

MOLNFT AF v1 smart contract in GenesisL1 blockchain:

0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba

IPFS of NFT metadata:

bafybeigpl7zkdyohu5rqnmppyl3l4qbzbxk2dg66y7zac7a7a776dmou7y/metadata.json

IPFS of structure file:

bafybeiecziu26az4aydlcqdfkqeqkencynj63sezczn2p52kixlh46m3ry/1drb.pdb

MOLNFT PDB v1

NFT id:
4549
PDB ID:
1DRB
Name:
CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL CHANGES AND COOPERATIVITY IN BINDING
Keywords:
OXIDOREDUCTASE
Experimental Method:
X-RAY DIFFRACTION
Resolution:
1.96

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 1DRB research and analysis (ICN3D with VR)

FASTA sequences

>1drb_A mol:protein length:159 DIHYDROFOLATE REDUCTASE
MISLIAALAVDRVIGMENAMPWNLPACLAWFKRNTLDKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR
>1drb_B mol:protein length:159 DIHYDROFOLATE REDUCTASE
MISLIAALAVDRVIGMENAMPWNLPACLAWFKRNTLDKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR

References and links

Current molecular structure file and data about current molecular structure file and NFT token based on it with
PDBID: 1DRB
TITLE: CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL CHANGES AND COOPERATIVITY IN BINDING
DOI: 10.1021/bi00222a028
AUTHORS: David, C., Kraut, J.
ACCESSION DATE: 11/06/91
Obtained at RCSB PDB https://rcsb.org
RCSB Link: https://www.rcsb.org/structure/1DRB