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3ILN

X-ray structure of the laminarinase from Rhodothermus marinus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 300
ChainResidue
ATRP107
AHOH422
AALA109
ATRP111
AGLU129
AASP131
AGLU134
AHOH269
AHOH369
AHOH380

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ATRP11
AARG186
ATRP255
AHOH282
AHOH450
AHOH454
AHOH516

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AGLU18
AGLY60
AASP248
AHOH382
AHOH492

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 400
ChainResidue
BGLU18
BGLY60
BASP248
BHOH365
BHOH561

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 300
ChainResidue
BASN41
BTRP107
BALA109
BTRP111
BGLU129
BASP131
BGLU134
BHOH258
BHOH395
BHOH408
BHOH517

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
BTRP11
BTHR181
BARG186
BTRP255
BHOH407
BHOH492

Functional Information from PROSITE/UniProt
site_idPS01034
Number of Residues12
DetailsGH16_1 Glycosyl hydrolases family 16 active sites. EIDIaEhvGFnP
ChainResidueDetails
AGLU129-PRO140

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PDB entries from 2024-07-31

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