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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
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:31316802
ChainResidueDetails
AASP182
BASP182
CASP182
DASP182

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:31316802
ChainResidueDetails
AGLU419
BGLU419
CGLU419
DGLU419

site_idSWS_FT_FI3
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:31316802
ChainResidueDetails
ATYR36
BTRP40
BTYR88
BGLN115
BGLY180
BARG216
BTYR375
BGLN434
CTYR36
CTRP40
CTYR88
ATRP40
CGLN115
CGLY180
CARG216
CTYR375
CGLN434
DTYR36
DTRP40
DTYR88
DGLN115
DGLY180
ATYR88
DARG216
DTYR375
DGLN434
AGLN115
AGLY180
AARG216
ATYR375
AGLN434
BTYR36

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PDB entries from 2024-09-11

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