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4JJ6

Crystal structure of a catalytic mutant of Axe2 (Axe2-H194A), an acetylxylan esterase from Geobacillus stearothermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004622molecular_functionlysophospholipase activity
A0005737cellular_componentcytoplasm
A0045493biological_processxylan catabolic process
A0046555molecular_functionacetylxylan esterase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
B0000272biological_processpolysaccharide catabolic process
B0004622molecular_functionlysophospholipase activity
B0005737cellular_componentcytoplasm
B0045493biological_processxylan catabolic process
B0046555molecular_functionacetylxylan esterase activity
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AGLY28
ASER29
AHOH435
AHOH498
AHOH538
AHOH637

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AHOH408
AHOH591
AHOH610
AHOH636
AHOH636
ATYR109
ATYR109
AASP111

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AGLN160
AGLN160
AGLU163
AGLU164
AHOH572
AHOH576
AHOH632

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
ACYS19
ATHR35
AGLY36
APRO195
ASER196
AVAL197
AHOH471
AHOH508
AHOH524
AHOH640

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 305
ChainResidue
ASER15
AGLY63
AASN92

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
BCYS19
BTHR35
BPRO195
BSER196
BVAL197
BHOH654
BHOH656

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 302
ChainResidue
BSER15
BGLY63
BASN92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:21994937, ECO:0000305|PubMed:24531461
ChainResidueDetails
ASER15
BSER15

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:21994937, ECO:0000305|PubMed:24531461
ChainResidueDetails
AASP191
AALA194
BASP191
BALA194

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:24531461
ChainResidueDetails
AGLY63
AASN92
BGLY63
BASN92

219869

PDB entries from 2024-05-15

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