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4CRY

Direct visualisation of strain-induced protein post-translational modification

Functional Information from GO Data
ChainGOidnamespacecontents
A0004068molecular_functionaspartate 1-decarboxylase activity
A0006523biological_processalanine biosynthetic process
B0005515molecular_functionprotein binding
B0015940biological_processpantothenate biosynthetic process
B0016485biological_processprotein processing
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0031638biological_processzymogen activation
B1905502molecular_functionacetyl-CoA binding
G0004068molecular_functionaspartate 1-decarboxylase activity
G0006523biological_processalanine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ACO B 1128
ChainResidue
BTRP23
BARG75
BGLY76
BVAL77
BGLY78
BGLN79
BGLY101
BVAL102
BGLU103
BMET108
BALA110
BGLU25
BPHE111
BMG1129
BHOH2032
BHOH2035
BHOH2038
BHOH2055
BHOH2056
GARG102
BTYR26
BSER65
BLEU66
BARG67
BVAL68
BARG73
BARG74

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 1129
ChainResidue
BTHR72
BARG73
BARG74
BARG75
BGLY76
BVAL77
BACO1128

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1130
ChainResidue
AHOH2004
AHOH2004

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues126
DetailsDomain: {"description":"N-acetyltransferase","evidences":[{"source":"HAMAP-Rule","id":"MF_02018","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues15
DetailsRegion: {"description":"Interaction with PanD","evidences":[{"source":"PubMed","id":"25910242","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02018","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25910242","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2008","submissionDatabase":"PDB data bank","title":"Solution NMR structure of putative N-acetyl transferase YhhK from E. coli bound to coenzyme A.","authors":["Cort J.R.","Yee A.","Arrowsmith C.H.","Kennedy M.A."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2014","submissionDatabase":"PDB data bank","title":"Direct visualisation of strain-induced protein post-translational modification.","authors":["Monteiro D.C.F.","Patel V.","Bartlett C.P.","Grant T.D.","Nozaki S.","Gowdy J.A.","Snell E.H.","Niki H.","Pearson A.R.","Webb M.E."]}},{"source":"PDB","id":"2K5T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Schiff-base intermediate with substrate; via pyruvic acid","evidences":[{"source":"PubMed","id":"9546220","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Pyruvic acid (Ser)","evidences":[{"source":"PubMed","id":"9546220","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 409
ChainResidueDetails
ALYS9electrostatic stabiliser

238895

PDB entries from 2025-07-16

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