Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6YDD

X-ray structure of LPMO.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:29057953, ECO:0000269|PubMed:32818374, ECO:0007744|PDB:5NLT, ECO:0007744|PDB:6YDC, ECO:0007744|PDB:6YDD, ECO:0007744|PDB:6YDE, ECO:0007744|PDB:6YDF
ChainResidueDetails
AHIC306
AHIS79
ATYR169
BHIC304
BHIS79
BTYR169

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:32818374, ECO:0007744|PDB:6YDE
ChainResidueDetails
AGLY45
BGLY45

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:32818374, ECO:0007744|PDB:6YDC, ECO:0007744|PDB:6YDD, ECO:0007744|PDB:6YDE
ChainResidueDetails
AASP76
ASER78
AASP155
BASP76
BSER78
BASP155

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q1K8B6
ChainResidueDetails
AHIS152
BHIS152

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon