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5H2G

Crystal structure of oxidized DapF from Corynebacterium glutamicum

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0008837molecular_functiondiaminopimelate epimerase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016853molecular_functionisomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0008837molecular_functiondiaminopimelate epimerase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0016853molecular_functionisomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 301
ChainResidue
AARG40
AASP47
AGLU217
ATHR218
AARG219
BARG41

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 302
ChainResidue
AHOH552
BARG40
BARG41
AARG40
AARG41
AHOH542

Functional Information from PROSITE/UniProt
site_idPS01326
Number of Residues15
DetailsDAP_EPIMERASE Diaminopimelate epimerase signature. NaDGSlaemCGNGvR
ChainResidueDetails
AASN74-ARG88

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"OCT-2016","submissionDatabase":"PDB data bank","title":"Crystal structure of reduced DapF from Corynebacterium glutamicum.","authors":["Sagong H.-Y.","Kim K.-J."]}},{"source":"PDB","id":"5M47","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00197","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2016","submissionDatabase":"PDB data bank","title":"Crystal structure of reduced DapF from Corynebacterium glutamicum.","authors":["Sagong H.-Y.","Kim K.-J."]}},{"source":"PDB","id":"5M47","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00197","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Could be important to modulate the pK values of the two catalytic cysteine residues","evidences":[{"source":"HAMAP-Rule","id":"MF_00197","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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