Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2D1Z

Crystal structure of catalytic-site mutant xylanase from Streptomyces olivaceoviridis E-86

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1441
ChainResidue
BSER631
BARG639
BASP640
BHOH2005
BHOH2094
BHOH2299

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1442
ChainResidue
AASP140
ASER131
AASP132
AARG139

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1443
ChainResidue
ATYR172
AASN173
AHIS207
AASN209
AARG275
AHOH1571
AHOH1820
AHOH1847

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 1444
ChainResidue
AGLU357
AARG359
ATRP383
AGLY384
AHOH1528
AHOH1676
AHOH1709
BALA855
BGLU857
BGLY884
BLYS889

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1445
ChainResidue
AASP408
AALA409
AGLY411
AGLY412
AGLN421
ATYR423
AASN430

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1446
ChainResidue
AASP325
AVAL326
APRO327
AASN328
AGLN338
ATYR340
AHIS343
AASN347
AHOH1660
AHOH1870

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1941
ChainResidue
BSER597
BARG645
BHOH1986
BHOH2206
BHOH2233

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1942
ChainResidue
BLYS548
BTRP585
BGLN588
BHIS628
BHOH2109
BHOH2391
BHOH2394

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1943
ChainResidue
BLYS524
BTHR771
BASP772
BSER773
BHOH1978
BHOH2097
BHOH2189

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1944
ChainResidue
BTYR672
BASN673
BHIS707
BASN709
BARG775
BHOH2109
BHOH2261
BHOH2418

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1945
ChainResidue
BASP825
BASN828
BTYR840
BHIS843
BASN847
BHOH2369

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1946
ChainResidue
BASP908
BALA909
BVAL910
BGLY911
BGLY912
BGLN921
BTYR923
BASN930

Functional Information from PROSITE/UniProt
site_idPS00591
Number of Residues11
DetailsGH10_1 Glycosyl hydrolases family 10 (GH10) active site. GVDVaITELDI
ChainResidueDetails
AGLY229-ILE239

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 2his
ChainResidueDetails
AHIS128

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 2his
ChainResidueDetails
BHIS628

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon