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

1R86

Crystal structure of the extracellular xylanase from Geobacillus stearothermophilus T-6 (XT6, monoclinic form): The E159A/E265A mutant at 1.8A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 901
ChainResidue
AHIS11
AGLU27
AASP365
ACL701

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 902
ChainResidue
AHOH1165
AASP21
AHOH1001
AHOH1162
AHOH1163
AHOH1164

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 903
ChainResidue
AASP282
AHIS378
AHOH1232
AHOH1298
AHOH1299

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 904
ChainResidue
AASP282
AHIS378
AHOH1274
AHOH1303
AHOH1347

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 905
ChainResidue
AGLU58
AHIS322
ACL702
AHOH1099

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 906
ChainResidue
AGLU27
ASER307
AILE310
AHOH1066
AHOH1231
AHOH1233

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 907
ChainResidue
AASP297
AALA374
AASP377
ALYS379
AHOH1018
AHOH1297
AHOH1331

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 701
ChainResidue
AHIS11
AASN26
AGLU27
AASP365
AZN901
AHOH1274

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 702
ChainResidue
AGLU58
AHIS322
ATRP324
AZN905
AHOH1071

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
AASP377
AHIS378
ALYS379

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AALA159

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10061
ChainResidueDetails
AALA265

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 2his
ChainResidueDetails
AALA159

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon