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

3RM8

AMCase in complex with Compound 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008061molecular_functionchitin binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008061molecular_functionchitin binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RM8 A 417
ChainResidue
ATRP99
ATRP360
ALEU364
AHOH584
AHOH588
AASP138
AGLU140
AMET210
ATYR212
AASP213
ATYR267
AGLU297
AILE300

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RM8 B 417
ChainResidue
BTRP99
BASP138
BGLU140
BALA183
BMET210
BTYR212
BASP213
BTYR267
BGLU297
BILE300
BTRP360
BHOH595
BHOH628

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGLDFDwE
ChainResidueDetails
APHE132-GLU140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLU140
BGLU140

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLU70
AGLY97
ATRP360
BGLU70
BGLY97
BTYR141
BMET210
BTRP360
ATYR141
AMET210

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon