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6H8L

Structure of peptidoglycan deacetylase PdaC from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0005975biological_processcarbohydrate metabolic process
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 501
ChainResidue
AASP286
AHIS336
AHIS340
ATLA502

site_idAC2
Number of Residues14
Detailsbinding site for residue TLA A 502
ChainResidue
APRO376
ATYR377
AGLY378
ATRP395
ALEU425
AHIS427
AZN501
BGLU468
BARG471
AASP285
AASP286
AHIS336
AHIS340
AARG374

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 501
ChainResidue
BASP286
BHIS336
BHIS340
BTLA502

site_idAC4
Number of Residues14
Detailsbinding site for residue TLA B 502
ChainResidue
AGLU468
AARG471
BASP285
BASP286
BHIS336
BHIS340
BARG374
BPRO376
BTYR377
BGLY378
BTRP395
BLEU425
BHIS427
BZN501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues348
DetailsDomain: {"description":"NodB homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU01014","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Raises pKa of active site His","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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