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6ZJP

Cold-adapted beta-D-galactosidase from Arthrobacter sp. 32cB mutant E517Q

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0005990biological_processlactose catabolic process
A0009056biological_processcatabolic process
A0009341cellular_componentbeta-galactosidase complex
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue NA A 1101
ChainResidue
AASP207
APHE581
AASP584
AHOH1598
AHOH1681

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 1102
ChainResidue
AALA957
AHOH1753
AARG913
APRO914
ALEU954
AASP955

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 1103
ChainResidue
AGLU393
AHIS395
AGLU441
AHOH1269
AHOH1275
AHOH1570

site_idAC4
Number of Residues7
Detailsbinding site for residue ACT A 1104
ChainResidue
APRO46
AALA47
AARG421
AHOH1219
AHOH1272
AHOH1358
AHOH1405

Functional Information from PROSITE/UniProt
site_idPS00608
Number of Residues15
DetailsGLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHASVVMWSlg.NE
ChainResidueDetails
AASP427-GLU441

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaIRTSHYPphpqFLalaDqlGFYVV
ChainResidueDetails
AASN362-VAL387

224201

PDB entries from 2024-08-28

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