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4PEW

Structure of sacteLam55A from Streptomyces sp. SirexAA-E

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
A0005576cellular_componentextracellular region
A0009251biological_processglucan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0000272biological_processpolysaccharide catabolic process
B0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
B0005576cellular_componentextracellular region
B0009251biological_processglucan catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 701
ChainResidue
AHOH996
AHOH1004
AHOH1022
AHOH1038
AHOH1043
AHOH1066

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 702
ChainResidue
AHOH1237
AHOH1270
AHOH1327
AHOH1115
AHOH1124
AHOH1187

site_idAC3
Number of Residues6
Detailsbinding site for residue MG B 701
ChainResidue
BHOH1022
BHOH1034
BHOH1049
BHOH1062
BHOH1107
BHOH1111

site_idAC4
Number of Residues8
Detailsbinding site for residue EDO B 702
ChainResidue
BPHE94
BGLY95
BARG98
BTYR118
BTHR358
BASP384
BARG418
BHOH1453

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:25752603
ChainResidueDetails
AGLU502
BGLU502

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:25752603
ChainResidueDetails
AGLN174
BTRP446
BGLU480
BTYR505
ATYR194
AGLN217
ATRP446
AGLU480
ATYR505
BGLN174
BTYR194
BGLN217

223790

PDB entries from 2024-08-14

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