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5NCD

Crystal structure of the polysaccharide deacetylase Bc1974 from Bacillus cereus in complex with (2S)-2-amino-5-(diaminomethylideneamino)-N-hydroxypentanamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
B0005886cellular_componentplasma membrane
B0005975biological_processcarbohydrate metabolic process
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0046872molecular_functionmetal ion binding
C0005886cellular_componentplasma membrane
C0005975biological_processcarbohydrate metabolic process
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0046872molecular_functionmetal ion binding
D0005886cellular_componentplasma membrane
D0005975biological_processcarbohydrate metabolic process
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue ACT A 301
ChainResidue
AASP76
AHIS126
AHIS130
APRO166
ATYR167
AHIS230
AZN302
DHIS269

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS126
AHIS130
AACT301
AHOH431
AASP77

site_idAC3
Number of Residues10
Detailsbinding site for residue AHL B 301
ChainResidue
BASP76
BASP77
BHIS126
BHIS130
BPRO166
BTYR167
BLEU228
BHIS230
BZN302
BHOH423

site_idAC4
Number of Residues5
Detailsbinding site for residue ZN B 302
ChainResidue
BASP77
BHIS126
BHIS130
BAHL301
BHOH423

site_idAC5
Number of Residues6
Detailsbinding site for residue CIT B 303
ChainResidue
BTRP191
BTHR192
BILE193
BASN219
BPHE267
CMET170

site_idAC6
Number of Residues8
Detailsbinding site for residue ACT C 301
ChainResidue
BHIS269
CASP76
CHIS126
CHIS130
CTYR167
CHIS230
CZN302
CHOH415

site_idAC7
Number of Residues5
Detailsbinding site for residue ZN C 302
ChainResidue
CASP77
CHIS126
CHIS130
CACT301
CHOH415

site_idAC8
Number of Residues8
Detailsbinding site for residue ACT D 301
ChainResidue
DASP76
DHIS126
DHIS130
DPRO166
DTYR167
DHIS230
DZN302
DHOH412

site_idAC9
Number of Residues5
Detailsbinding site for residue ZN D 302
ChainResidue
DASP77
DHIS126
DHIS130
DACT301
DHOH412

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues744
DetailsDomain: {"description":"NodB homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU01014","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"29257674","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"29257674","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29257674","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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