Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5EUV

Crystal structure of a cold-adapted dimeric beta-D-galactosidase from Paracoccus sp. 32d strain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue ACT A 801
ChainResidue
AARG545
BHOH961

site_idAC2
Number of Residues3
Detailsbinding site for residue ACT A 803
ChainResidue
AHIS291
AILE316
AHOH1034

site_idAC3
Number of Residues5
Detailsbinding site for residue BTB A 804
ChainResidue
BVAL665
AGLN333
AASP337
BGLU628
BGLN664

site_idAC4
Number of Residues6
Detailsbinding site for residue PEG A 805
ChainResidue
APRO612
AGLY613
AARG614
AHOH1186
AHOH1191
AHOH1203

site_idAC5
Number of Residues8
Detailsbinding site for residue PEG A 806
ChainResidue
AARG545
ALEU603
AGLN605
ATRP606
ASER609
ATRP610
AHOH946
AHOH1081

site_idAC6
Number of Residues2
Detailsbinding site for residue ACT B 801
ChainResidue
BHIS291
BILE316

site_idAC7
Number of Residues1
Detailsbinding site for residue ACT B 802
ChainResidue
BHOH1141

site_idAC8
Number of Residues7
Detailsbinding site for residue ACT B 803
ChainResidue
BASP134
BTRP327
BASN364
BGLU365
BGLU446
BTRP489
BHOH1133

site_idAC9
Number of Residues3
Detailsbinding site for residue ACT B 804
ChainResidue
BMET400
BLYS438
BACT805

site_idAD1
Number of Residues3
Detailsbinding site for residue ACT B 805
ChainResidue
BARG381
BMET400
BACT804

Functional Information from PROSITE/UniProt
site_idPS00608
Number of Residues16
DetailsGLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DWNHPSIVIWGvriNE
ChainResidueDetails
AASP350-GLU365

site_idPS00719
Number of Residues26
DetailsGLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NmVRTSHYPqstwFLdrcDeiGLLVF
ChainResidueDetails
AASN296-PHE321

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon