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5EER

Crystal structure of DapB from Corynebacterium glutamicum

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008839molecular_function4-hydroxy-tetrahydrodipicolinate reductase
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016491molecular_functionoxidoreductase activity
A0016726molecular_functionoxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
A0019877biological_processdiaminopimelate biosynthetic process
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 301
ChainResidue
ALYS138
ASER143
AGLY144
ATHR145

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 A 302
ChainResidue
AHIS135
ALYS138

Functional Information from PROSITE/UniProt
site_idPS01298
Number of Residues18
DetailsDAPB Dihydrodipicolinate reductase signature. EViElHhpnKlDapSGTA
ChainResidueDetails
AGLU129-ALA146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00102
ChainResidueDetails
AHIS134

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00102
ChainResidueDetails
ALYS138

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00102
ChainResidueDetails
AGLY9
AGLY77
AALA104
AHIS135
AGLY144

224931

PDB entries from 2024-09-11

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