3RIS PDB NFT
Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme
MOLNFT AF v1 smart contract in GenesisL1 blockchain:
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
IPFS of NFT metadata:
bafybeihmi2s2fjia5vikvn56vcxuapcfgwqieieq3o7v4nku7bpfjtmlvu/metadata.json
IPFS of structure file:
bafybeifpd4crhsaaj73u5jpeqmhsbglsv67ti62iko2ttuq4qgr2ah4d4i/3ris.pdb
MOLNFT 3RIS research and analysis (ICN3D with VR)
FASTA sequences
>3ris_A mol:protein length:245 Ubiquitin carboxyl-terminal hydrolase isozyme L5
GPLGSMTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQR
>3ris_B mol:protein length:245 Ubiquitin carboxyl-terminal hydrolase isozyme L5
GPLGSMTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQR
>3ris_C mol:protein length:245 Ubiquitin carboxyl-terminal hydrolase isozyme L5
GPLGSMTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQR
>3ris_D mol:protein length:245 Ubiquitin carboxyl-terminal hydrolase isozyme L5
GPLGSMTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQR
References and links
Current molecular structure file and data about current molecular structure file and NFT token based on it with
PDBID: 3RIS
TITLE: Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme
DOI: 10.1111/j.1742-4658.2011.08393.x
AUTHORS: Das, C., Permaul, M., Maiti, T.K.
ACCESSION DATE: 04/14/11
Obtained at RCSB PDB https://rcsb.org
RCSB Link: https://www.rcsb.org/structure/3RIS