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2W8R

The crystal structure of human SSADH in complex with NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004777molecular_functionsuccinate-semialdehyde dehydrogenase (NAD+) activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006105biological_processsuccinate metabolic process
A0006536biological_processglutamate metabolic process
A0007417biological_processcentral nervous system development
A0009013molecular_functionsuccinate-semialdehyde dehydrogenase [NAD(P)+] activity
A0009448biological_processgamma-aminobutyric acid metabolic process
A0009450biological_processgamma-aminobutyric acid catabolic process
A0009791biological_processpost-embryonic development
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0042802molecular_functionidentical protein binding
A0045202cellular_componentsynapse
A0051932biological_processsynaptic transmission, GABAergic
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ADP A 702
ChainResidue
ATHR202
ATHR288
ATRP204
ALYS228
AALA230
AGLU231
AALA264
AGLY268
APHE282
ASER285

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
ALEU368
AARG369
AVAL370
AHIS413

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
AGLN349
AASP450
ATHR451
AGLU452

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
ALEU51
AARG68
ASER83

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
AARG350
ALYS448

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 1005
ChainResidue
AHOH2048

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1006
ChainResidue
ATYR159
APHE206
AARG334
ASER498

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1007
ChainResidue
AVAL95
AARG96
AARG261
ALYS262

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1008
ChainResidue
AVAL65
ALEU70
AGLY84
ALYS417

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 1009
ChainResidue
AARG60

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1010
ChainResidue
ATYR159
AARG213
AARG334
AVAL341
ASER498
APHE504

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1101
ChainResidue
ATHR408
AGLY409

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1102
ChainResidue
AARG103
AASN385
AGLU386

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGLAP
ChainResidueDetails
AMET305-PRO312

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007
ChainResidueDetails
AGLU306

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10008
ChainResidueDetails
AALA340

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P20000
ChainResidueDetails
AGLU306
AGLU438
ATHR202

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19300440, ECO:0007744|PDB:2W8Q
ChainResidueDetails
AARG334
ASER498
AARG213

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19300440, ECO:0007744|PDB:2W8R
ChainResidueDetails
ALYS228
AGLY284

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000
ChainResidueDetails
AASN205

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8BWF0
ChainResidueDetails
ALYS265
ALYS126

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8BWF0
ChainResidueDetails
ALYS402
ALYS135
ALYS184

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BWF0
ChainResidueDetails
ALYS365
ALYS411

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER499

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PDB entries from 2024-06-12

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