Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1EB9

Structure Determinants of Substrate Specificity of Hydroxynitrile Lyase from Manihot esculenta

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0047606molecular_functionhydroxynitrilase activity
A0052891molecular_functionaliphatic (S)-hydroxynitrile lyase activity
A0052892molecular_functionaromatic (S)-hydroxynitrile lyase activity
B0016829molecular_functionlyase activity
B0047606molecular_functionhydroxynitrilase activity
B0052891molecular_functionaliphatic (S)-hydroxynitrile lyase activity
B0052892molecular_functionaromatic (S)-hydroxynitrile lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HBA A1259
ChainResidue
ATHR11
AILE12
ASER80
ACYS81
AMET147
ALEU179
AHBA1260
AHOH2123
AHOH2132

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HBA A1260
ChainResidue
APHE125
AILE210
AHBA1259
AHOH2123

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HBA B1259
ChainResidue
BTHR11
BILE12
BSER80
BCYS81
BMET147
BHBA1260
BHOH2138
BHOH2139

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HBA B1260
ChainResidue
BLEU122
BPHE125
BALA128
BILE210
BHBA1259
BHOH2139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:11173464, ECO:0000305|PubMed:11316882
ChainResidueDetails
ACYS81
ALYS237
BCYS81
BLYS237

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11173464, ECO:0007744|PDB:1DWO
ChainResidueDetails
AILE12
ACYS81
AALA82
BILE12
BCYS81
BALA82

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Increases basicity of active site His => ECO:0000305|PubMed:11316882
ChainResidueDetails
ALYS209
BLYS209

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
ASER80
AHIS236
AASP208
ATHR11

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
BSER80
BHIS236
BASP208
BTHR11

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
ASER80
AHIS236
AASP208

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c4x
ChainResidueDetails
BSER80
BHIS236
BASP208

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon