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5M16

Structure of GH36 alpha-galactosidase from Thermotoga maritima in complex with a hydrolysed cyclopropyl carbasugar.

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 Residues8
Detailsbinding site for residue SO4 A 601
ChainResidue
AARG9
AGLY393
AGLU394
AHOH711
AHOH793
AHOH797
AHOH867
AHOH877

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 602
ChainResidue
AASP303
AGLU304
ALYS339
ALYS302

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 603
ChainResidue
AASP419
AASP454
AHOH723
AHOH909
AHOH953
AHOH955

site_idAC4
Number of Residues13
Detailsbinding site for residue 7D2 A 604
ChainResidue
ASER-4
ATRP65
ATRP190
ATYR191
AASP220
AASP221
ATRP257
ALYS325
AASP327
ACYS368
AARG383
AASP387
AHOH720

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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