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5M0X

Structure of apo structure of GH36 alpha-galactosidase from Thermotoga maritima

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004557molecular_functionalpha-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0016139biological_processglycoside catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 601
ChainResidue
AASP419
AASP454
AHOH752
AHOH857
AHOH871
AHOH873

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 602
ChainResidue
AGLU394
AHIS395
AHOH705
AHOH713
AHOH811
AARG9
APHE391
AGLY393

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 603
ChainResidue
AGLU434
ALYS435
ATHR436

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 604
ChainResidue
ALYS302
AASP303
AGLU304
ALYS339

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
AASP220
ALYS325
ACYS368
AARG383

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PDB entries from 2024-07-17

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