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6C8W

Crystal structure of Aspartate Semialdehyde Dehydrogenase with NADP from Blastomyces dermatitidis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
A0006520biological_processamino acid metabolic process
A0008652biological_processamino acid biosynthetic process
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0046983molecular_functionprotein dimerization activity
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
B0006520biological_processamino acid metabolic process
B0008652biological_processamino acid biosynthetic process
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0046983molecular_functionprotein dimerization activity
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue NAP A 401
ChainResidue
AGLY13
ALEU87
AASP88
APRO89
AALA91
AASN109
AALA110
ASER185
AGLY186
AGLY188
AASN340
ATHR15
ATHR341
AALA345
AHOH525
AHOH540
AGLY16
AALA17
AVAL18
AALA39
ASER40
ASER43
AGLY86

site_idAC2
Number of Residues20
Detailsbinding site for residue NAP B 401
ChainResidue
BGLY13
BTHR15
BGLY16
BALA17
BVAL18
BALA39
BSER40
BSER43
BGLY86
BLEU87
BASP88
BPRO89
BALA91
BASN109
BALA110
BASN153
BCYS154
BGLY188
BGLU208
BLYS211

Functional Information from PROSITE/UniProt
site_idPS01103
Number of Residues15
DetailsASD Aspartate-semialdehyde dehydrogenase signature. VSvaCnRVpvldGHT
ChainResidueDetails
AVAL238-THR252

223790

PDB entries from 2024-08-14

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