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4KNA

Crystal structure of an N-succinylglutamate 5-semialdehyde dehydrogenase from Burkholderia thailandensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0006525biological_processarginine metabolic process
A0006527biological_processarginine catabolic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0019544biological_processarginine catabolic process to glutamate
A0019545biological_processarginine catabolic process to succinate
A0043824molecular_functionsuccinylglutamate-semialdehyde dehydrogenase activity
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0006525biological_processarginine metabolic process
B0006527biological_processarginine catabolic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0019544biological_processarginine catabolic process to glutamate
B0019545biological_processarginine catabolic process to succinate
B0043824molecular_functionsuccinylglutamate-semialdehyde dehydrogenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
AARG420
AHOH996
BARG134

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
ATHR400
AALA401
APHE402
AARG424
AGLY447
ACA504

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AARG282
AGLU375
AHIS377
APHE378

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 504
ChainResidue
ATHR400
AEDO502
AHOH951
AHOH952

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 501
ChainResidue
AARG134
AMET467
BARG420

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 502
ChainResidue
BARG282
BALA334
BHIS377
BPHE378

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 503
ChainResidue
BTHR400
BALA401
BPHE402
BARG424
BCA504

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 504
ChainResidue
BTHR400
BEDO503
BHOH678
BHOH1035

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FlSAGQRCTCAR
ChainResidueDetails
APHE271-ARG282

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LEMGGNNP
ChainResidueDetails
ALEU243-PRO250

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01174
ChainResidueDetails
AGLU244
ACYS278
BGLU244
BCYS278

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01174
ChainResidueDetails
AGLY221
BGLY221

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PDB entries from 2024-07-17

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