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6JQB

The structure of maltooligosaccharide-forming amylase from Pseudomonas saccharophila STB07 with pseudo-maltoheptaose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004556molecular_functionalpha-amylase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0005983biological_processstarch catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
A0033910molecular_functionglucan 1,4-alpha-maltotetraohydrolase activity
A0043169molecular_functioncation binding
A0046872molecular_functionmetal ion binding
A2001070molecular_functionstarch binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO A 601
ChainResidue
AARG96
AGLY184
AGLY186
AHOH703
AHOH865
AHOH926

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 602
ChainResidue
AHOH873
AGLY300
AGLN301
AASN393

site_idAC3
Number of Residues33
Detailsbinding site for residue 7SA A 605
ChainResidue
ATRP25
ATRP66
ATYR78
APHE79
AHIS117
APHE156
AILE157
AGLY158
AGLU160
ASER161
AARG191
AASP193
APHE194
AARG196
AGLU219
ATRP221
AGLU226
ATRP238
AHIS293
AASP294
AGLN305
AHIS307
ATRP308
AHOH730
AHOH772
AHOH809
AHOH838
AHOH866
AHOH868
AHOH913
AHOH963
AHOH995
AHOH1011

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP193

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU219

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP1
AASP154
APHE156
AASP162
AARG191
AGLY197
AHIS293
AGLN305
AGLN2
AHIS13
AASP16
AGLU17
ATYR78
AASN116
AHIS117
AASP151

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP294

222624

PDB entries from 2024-07-17

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