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5OIV

Crystal structure of Mycolicibacterium hassiacum glucosylglycerate hydrolase (MhGgH) D43A 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
A0008152biological_processmetabolic process
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
B0008152biological_processmetabolic process
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 Residues9
Detailsbinding site for residue GOL A 501
ChainResidue
AGLN11
AARG125
AHIS129
AGLY446
AHOH654
AHOH664
AHOH754
BGLU399
BARG402

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 502
ChainResidue
AGLU399
AARG402
AHOH626
AHOH638
AHOH872
BGLN11
BARG125
BHIS129
BGLY446

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 503
ChainResidue
AMET153
AARG154
AARG157
AASP279
AHOH738

site_idAC4
Number of Residues9
Detailsbinding site for residue GOL A 504
ChainResidue
ATYR36
ATRP40
ATRP42
AGLN115
AGLN434
ASER510
AHOH639
AHOH671
AHOH690

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 505
ChainResidue
AHIS334
AHOH835
BGLN264
BTYR284

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL A 506
ChainResidue
AGLN264
ATYR284
BHIS334

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL A 507
ChainResidue
AILE210
AGLY430
AMET432
AHOH710
AHOH825

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL A 508
ChainResidue
ATYR202
AGLN203
AARG204
AASP223
AHOH687

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL A 509
ChainResidue
AGLU296
ATHR297
ATHR298
ATRP315
AHOH614

site_idAD1
Number of Residues10
Detailsbinding site for residue SER A 510
ChainResidue
ATRP40
AHIS78
ATYR88
AASP182
AARG216
ATYR222
ATYR375
AGOL504
AHOH630
AHOH667

site_idAD2
Number of Residues4
Detailsbinding site for residue GLY A 511
ChainResidue
AGLU345
AARG400
ALEU403
AHOH635

site_idAD3
Number of Residues4
Detailsbinding site for residue GLY A 512
ChainResidue
AARG338
AGLU345
AARG400
BASP272

site_idAD4
Number of Residues3
Detailsbinding site for residue GLY A 513
ChainResidue
AARG168
APHE308
ATRP315

site_idAD5
Number of Residues4
Detailsbinding site for residue GOL B 501
ChainResidue
BARG154
BARG157
BASP279
BHOH833

site_idAD6
Number of Residues9
Detailsbinding site for residue GOL B 502
ChainResidue
BTYR36
BTRP40
BTRP42
BGLN115
BGLN434
BSER504
BHOH616
BHOH694
BHOH727

site_idAD7
Number of Residues7
Detailsbinding site for residue GOL B 503
ChainResidue
BGLU296
BTHR297
BTHR298
BGLN300
BARG306
BTRP315
BHOH728

site_idAD8
Number of Residues9
Detailsbinding site for residue SER B 504
ChainResidue
BARG216
BTYR375
BGOL502
BHOH617
BHOH708
BTRP40
BHIS78
BTYR88
BASP182

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
AGLU419
BGLU419

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

218853

PDB entries from 2024-04-24

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