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1ZY9

Crystal structure of Alpha-galactosidase (EC 3.2.1.22) (Melibiase) (tm1192) from Thermotoga maritima at 2.34 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004557molecular_functionalpha-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0016139biological_processglycoside catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 553
ChainResidue
AILE3
ALYS6
ATHR7
APHE8
AARG9
APHE13
APHE24

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 554
ChainResidue
AASP387
AGLY400
AALA401
APRO402
ATRP65
APRO386

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 555
ChainResidue
ATRP65
AGLY400

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 556
ChainResidue
AASN290
ATRP291
AHOH597
AHOH692

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 557
ChainResidue
ATRP190
ATYR191
AASP220
ATRP257
ALYS325
AASP327
AARG383
AASP387

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:17323919
ChainResidueDetails
AASP327

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17323919
ChainResidueDetails
AASP387

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27783466, ECO:0007744|PDB:5M16
ChainResidueDetails
ATRP65
ATYR191
ACYS368
AARG383
AASP220
ALYS325

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PDB entries from 2024-04-17

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