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5TJR

X-ray Crystal structure of a methylmalonate semialdehyde dehydrogenase from Pseudomonas sp. AAC

Functional Information from GO Data
ChainGOidnamespacecontents
A0004491molecular_functionmethylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0004491molecular_functionmethylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0004491molecular_functionmethylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0004491molecular_functionmethylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
E0004491molecular_functionmethylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
E0016491molecular_functionoxidoreductase activity
E0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F0004491molecular_functionmethylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
F0016491molecular_functionoxidoreductase activity
F0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue ADP A 501
ChainResidue
ATHR146
ATYR231
APRO147
APHE148
ALYS172
AGLU175
AASP204
ALYS205
ASER225
AILE228

site_idAC2
Number of Residues10
Detailsbinding site for residue ADP B 501
ChainResidue
BTHR146
BPHE148
BASN149
BLYS172
BPRO173
BGLU175
BVAL208
BGLY224
BSER225
BILE228

site_idAC3
Number of Residues11
Detailsbinding site for residue ADP D 501
ChainResidue
DILE145
DTHR146
DPRO147
DPHE148
DLYS172
DPRO173
DGLU175
DARG176
DLYS205
DSER225
DILE228

site_idAC4
Number of Residues11
Detailsbinding site for residue ADP E 501
ChainResidue
ETHR146
EPRO147
EPHE148
EASN149
ELYS172
ESER174
EGLU175
ELYS205
EVAL208
ESER225
EILE228

site_idAC5
Number of Residues12
Detailsbinding site for residue ADP F 501
ChainResidue
FTHR146
FPHE148
FLYS172
FPRO173
FSER174
FGLU175
FARG176
FLYS205
FVAL208
FPHE222
FSER225
FILE228

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YgSCGERCMAIS
ChainResidueDetails
ATYR273-SER284

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PDB entries from 2024-10-09

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