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5OHZ

Crystal structure of Mycolicibacterium hassiacum glucosylglycerate hydrolase (MhGgH) - SeMet derivative

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
C0004573molecular_functionGlc3Man9GlcNAc2 oligosaccharide glucosidase activity
C0005975biological_processcarbohydrate metabolic process
C0006487biological_processprotein N-linked glycosylation
C0009311biological_processoligosaccharide metabolic process
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0102547molecular_functionglucosylglycerate hydrolase activity
D0004573molecular_functionGlc3Man9GlcNAc2 oligosaccharide glucosidase activity
D0005975biological_processcarbohydrate metabolic process
D0006487biological_processprotein N-linked glycosylation
D0009311biological_processoligosaccharide metabolic process
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0102547molecular_functionglucosylglycerate hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue GOL A 501
ChainResidue
ATYR36
ATRP40
ATRP42
AASP43
AGLN115
AGLN434
ATRP436
ASER505
AHOH615

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 502
ChainResidue
AGLU296
ATHR297
ATHR298
AARG306
ATRP315
AHOH702
AHOH784

site_idAC3
Number of Residues1
Detailsbinding site for residue GOL A 503
ChainResidue
AHIS334

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 504
ChainResidue
ATRP386
ASER389
ATRP390
AASP443
ATRP444
AHOH668
AHOH697
AHOH800

site_idAC5
Number of Residues11
Detailsbinding site for residue SER A 505
ChainResidue
ATRP40
AHIS78
ATYR88
AASP182
AARG216
ATYR222
ATYR375
AGOL501
AHOH607
AHOH625
AHOH643

site_idAC6
Number of Residues10
Detailsbinding site for residue GOL B 501
ChainResidue
BTYR36
BTRP40
BTRP42
BASP43
BGLN115
BTYR375
BGLN434
BTRP436
BSER507
BHOH673

site_idAC7
Number of Residues8
Detailsbinding site for residue GOL B 502
ChainResidue
AGLN11
BARG125
BHIS129
BGLY446
BHOH609
BHOH634
DGLU399
DARG402

site_idAC8
Number of Residues2
Detailsbinding site for residue GOL B 503
ChainResidue
BHIS334
DTYR284

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL B 504
ChainResidue
BTRP149
BGLY150
BMSE153
BPRO276
BASP279
BHOH759

site_idAD1
Number of Residues8
Detailsbinding site for residue GOL B 505
ChainResidue
BGLU296
BTHR297
BTHR298
BARG306
BTRP315
BHOH623
BHOH685
BHOH788

site_idAD2
Number of Residues8
Detailsbinding site for residue GOL B 506
ChainResidue
BTRP386
BSER389
BTRP390
BASP443
BTRP444
BHOH664
BHOH754
BHOH762

site_idAD3
Number of Residues11
Detailsbinding site for residue SER B 507
ChainResidue
BTRP40
BHIS78
BTYR88
BASP182
BARG216
BTYR222
BTYR375
BGOL501
BHOH618
BHOH652
BHOH689

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL C 501
ChainResidue
AARG125
AHIS129
AGLY446
BGLN11
CGLU399
CARG402
CHOH647

site_idAD5
Number of Residues8
Detailsbinding site for residue GOL C 502
ChainResidue
CASP43
CGLN115
CGLN434
CSER505
CHOH627
CTYR36
CTRP40
CTRP42

site_idAD6
Number of Residues7
Detailsbinding site for residue GOL C 503
ChainResidue
AGLU399
AARG402
CARG125
CHIS129
CGLY446
CHOH619
DGLN11

site_idAD7
Number of Residues6
Detailsbinding site for residue GOL C 504
ChainResidue
CTHR297
CTHR298
CASP299
CARG306
CTRP315
CHOH741

site_idAD8
Number of Residues9
Detailsbinding site for residue SER C 505
ChainResidue
CTYR36
CTRP40
CHIS78
CTYR88
CASP182
CARG216
CTYR375
CGOL502
CHOH644

site_idAD9
Number of Residues9
Detailsbinding site for residue GOL D 501
ChainResidue
DTYR36
DTRP40
DTRP42
DASP43
DGLN115
DGLN434
DTRP436
DSER503
DHOH636

site_idAE1
Number of Residues9
Detailsbinding site for residue GOL D 502
ChainResidue
BGLU399
BARG402
BHOH909
CGLN11
DARG125
DHIS129
DASP443
DGLY446
DHOH664

site_idAE2
Number of Residues10
Detailsbinding site for residue SER D 503
ChainResidue
DTRP40
DHIS78
DTYR88
DASP182
DARG216
DTYR222
DTYR375
DGOL501
DHOH612
DHOH706

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"31316802","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31316802","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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