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4AK5

Native crystal structure of BpGH117

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1403
ChainResidue
ATYR186
AASN192
ALYS242
AHIS244

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 1403
ChainResidue
BTYR186
BASN192
BLYS242
BHIS244
BHOH2106

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1404
ChainResidue
ATRP127
ATHR165
AGLN180
AHIS244
AHOH2127

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1404
ChainResidue
BTRP127
BPHE164
BTHR165
BGLN180
BHIS244
BHOH2106

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1405
ChainResidue
AHOH2085
AHOH2086
AHOH2087
AHOH2089
AHOH2293
AHOH2371

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 1405
ChainResidue
BPRO91
BHOH2069
BHOH2070
BHOH2071
BHOH2073
BHOH2240
BHOH2302

Functional Information from PROSITE/UniProt
site_idPS00146
Number of Residues16
DetailsBETA_LACTAMASE_A Beta-lactamase class-A active site. FeIMSVvKgapHAIGL
ChainResidueDetails
APHE336-LEU351

238895

PDB entries from 2025-07-16

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