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4PQ9

Crystal Structure of a Beta-1,3-glucanase from Mycobacterium marinum

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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AGLU35
ASER86
AASP253
AHOH407

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 302
ChainResidue
AGLY111
AARG242
AHOH511

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BTB A 303
ChainResidue
ATRP134
AGLU142
AASP144
AGLU147
ATYR149
AHOH421
AHOH533
AHOH602
AHOH650
ATRP130
AALA132

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AHOH421
AHOH441
AHOH535

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BGLU35
BSER86
BASP253
BHOH406

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BTB B 302
ChainResidue
BGLU56
BTRP130
BALA132
BTRP134
BGLU142
BASP144
BGLU147
BHOH539
BHOH639
BHOH658

Functional Information from PROSITE/UniProt
site_idPS01034
Number of Residues12
DetailsGH16_1 Glycosyl hydrolases family 16 active sites. EIDIiEwyGNgS
ChainResidueDetails
AGLU142-SER153

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PDB entries from 2024-05-29

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