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2WHJ

Understanding how diverse mannanases recognise heterogeneous substrates

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016985molecular_functionmannan endo-1,4-beta-mannosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1311
ChainResidue
AARG93
AASP94
ASER95
AASP98
AHOH2142
AHOH2375
AHOH2376
AHOH2377

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 1312
ChainResidue
AGLY134
ASER135
ATYR174
AHOH2226
AASP133

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 1313
ChainResidue
AARG96
ASER97
AHOH2378

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1318
ChainResidue
ATRP61
AASP268
AHOH2091
AHOH2370
AHOH2373

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 1314
ChainResidue
AHIS225
AGLU234
AARG280

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 1315
ChainResidue
AARG96
AASP139
AHOH2197

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1316
ChainResidue
ASER257
ATHR258
APRO309
ATHR310
AHOH2374
AHOH2379

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 1317
ChainResidue
AASP150
APRO183
AARG280
AGLY284
AALA285
AHOH2380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P22533
ChainResidueDetails
AGLU127

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P22533
ChainResidueDetails
AGLU222

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AHIS192
AASN126
AGLU222
AGLU127
ATYR194

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PDB entries from 2024-07-24

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