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

5BN1

Structure of Axe2-W215I, an acetyl xylan esterase from Geobacillus stearothermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004622molecular_functionphosphatidylcholine lysophospholipase A1 activity
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0045493biological_processxylan catabolic process
A0046555molecular_functionacetylxylan esterase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
B0000272biological_processpolysaccharide catabolic process
B0004622molecular_functionphosphatidylcholine lysophospholipase A1 activity
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0045493biological_processxylan catabolic process
B0046555molecular_functionacetylxylan esterase activity
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL A 301
ChainResidue
ATYR109
AASP111
AHOH411
AHOH411
AHOH504
AHOH504
AHOH512
AHOH570

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 302
ChainResidue
AGLY63
AASN92
AHOH596
ASER15

site_idAC3
Number of Residues5
Detailsbinding site for residue IMD A 303
ChainResidue
AARG205
AARG209
AGLU214
AILE215
AHOH417

site_idAC4
Number of Residues7
Detailsbinding site for residue IMD A 304
ChainResidue
AGLU114
AARG156
AGLN160
AGLU164
AHOH552
AHOH605
AHOH605

site_idAC5
Number of Residues3
Detailsbinding site for residue CL B 301
ChainResidue
BSER15
BGLY63
BASN92

site_idAC6
Number of Residues4
Detailsbinding site for residue IMD B 302
ChainResidue
BARG67
BGLU74
BGLU123
BHOH619

site_idAC7
Number of Residues5
Detailsbinding site for residue IMD B 303
ChainResidue
BARG205
BARG209
BGLU214
BILE215
BHOH540

site_idAC8
Number of Residues10
Detailsbinding site for residue TRS B 304
ChainResidue
APRO146
BGLU140
BGLY141
BASN142
BPRO185
BHOH418
BHOH436
BHOH441
BHOH494
BHOH549

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL B 305
ChainResidue
AGLU140
AGLY141
APRO185
AHOH439
AHOH443
BPRO146
BHOH582

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21994937","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24531461","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"21994937","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24531461","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"24531461","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon