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4QDM

Crystal structure of N-terminal mutant (V1L) of an alkali thermostable GH10 xylanase from Bacillus sp. NG-27

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASN292
AARG351
AASP354
AHOH514
AHOH535
AHOH682
AHOH695

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AGLY61
ATRP96
AARG125
ATHR128
AHIS129
AHOH643
AGLN57
AGLU60

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 403
ChainResidue
ASER18
AASP302
ALEU305
AHOH573
AHOH631

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASN292
BARG351
BASP354
BHOH529
BHOH542
BHOH701
BHOH708

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 402
ChainResidue
BGLN57
BGLU60
BGLY61
BTRP96
BARG125
BTHR128
BHIS129
BHOH656

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 403
ChainResidue
BSER18
BASP302
BLEU305
BHOH558
BHOH618
BHOH651

Functional Information from PROSITE/UniProt
site_idPS00591
Number of Residues11
DetailsGH10_1 Glycosyl hydrolases family 10 (GH10) active site. GLDNqVTELDV
ChainResidueDetails
AGLY252-VAL262

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PDB entries from 2024-07-17

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