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4E4P

Second native structure of Xylanase A1 from Paenibacillus sp. JDR-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP14
AALA296
AILE299
AHOH588
AHOH604

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 402
ChainResidue
AMG403
BARG108
BHOH538
ATHR60
APHE61
ATHR62
AALA63

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
ATHR60
APHE61
ATHR62
AALA63
AALA64
ACL402
AHOH612

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP14
BALA296
BILE299
BHOH579
BHOH593

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B 402
ChainResidue
AARG108
AHOH544
BTHR60
BTHR62
BALA63
BMG403

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 403
ChainResidue
BTHR60
BPHE61
BTHR62
BALA63
BALA64
BCL402
BHOH609

Functional Information from PROSITE/UniProt
site_idPS00591
Number of Residues11
DetailsGH10_1 Glycosyl hydrolases family 10 (GH10) active site. GVEVsVSELDV
ChainResidueDetails
AGLY255-VAL265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU138
BGLU138

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP193
BASP193

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10061
ChainResidueDetails
AGLU262
BGLU262

220472

PDB entries from 2024-05-29

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