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5OIE

Crystal structure of Mycolicibacterium hassiacum glucosylglycerate hydrolase (MhGgH) E419A variant in complex with serine and glycerol

Functional Information from GO Data
ChainGOidnamespacecontents
A0004573molecular_functionGlc3Man9GlcNAc2 oligosaccharide glucosidase activity
A0005975biological_processcarbohydrate metabolic process
A0006487biological_processprotein N-linked glycosylation
A0009311biological_processoligosaccharide metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0102547molecular_functionglucosylglycerate hydrolase activity
B0004573molecular_functionGlc3Man9GlcNAc2 oligosaccharide glucosidase activity
B0005975biological_processcarbohydrate metabolic process
B0006487biological_processprotein N-linked glycosylation
B0009311biological_processoligosaccharide metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0102547molecular_functionglucosylglycerate hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 501
ChainResidue
ATYR36
ATRP40
ATRP42
AASP43
AGLN115
AGLN434
ASER507

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 502
ChainResidue
AASP279
AHOH757
AARG154
AARG157

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 503
ChainResidue
AGLU399
AARG402
BGLN11
BARG125
BHIS129

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 504
ChainResidue
ATHR297
ATHR298
AARG306
ATRP315

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL A 506
ChainResidue
AHIS334
BTYR284

site_idAC6
Number of Residues12
Detailsbinding site for residue SER A 507
ChainResidue
ATYR36
ATRP40
AHIS78
ATYR88
AASP182
AARG216
ATYR222
ATYR375
AGOL501
AHOH623
AHOH641
AHOH665

site_idAC7
Number of Residues6
Detailsbinding site for residue PEG A 508
ChainResidue
ATYR202
AGLN203
AARG204
AASN207
AASP219
AHOH689

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL B 501
ChainResidue
BTYR36
BTRP40
BTRP42
BASP43
BGLN115
BGLN434
BSER505

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL B 502
ChainResidue
BARG154
BARG157
BPRO276
BASP279
BHOH675

site_idAD1
Number of Residues7
Detailsbinding site for residue GOL B 503
ChainResidue
AGLN11
AARG125
AHIS129
AHOH620
BGLU399
BARG402
BHOH704

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL B 504
ChainResidue
BGLU296
BTHR297
BTHR298
BGLN300
BARG306

site_idAD3
Number of Residues10
Detailsbinding site for residue SER B 505
ChainResidue
BTYR36
BTRP40
BHIS78
BTYR88
BASP182
BARG216
BTYR222
BTYR375
BGOL501
BHOH618

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:31316802
ChainResidueDetails
AASP182
BASP182

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:31316802
ChainResidueDetails
AALA419
BALA419

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:31316802
ChainResidueDetails
BTYR88
BGLN115
BGLY180
BARG216
BTYR375
BGLN434
AGLN434
BTYR36
BTRP40
ATYR36
ATRP40
ATYR88
AGLN115
AGLY180
AARG216
ATYR375

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PDB entries from 2024-05-15

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