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3Q3C

Crystal structure of a serine dehydrogenase from Pseudomonas aeruginosa pao1 in complex with NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0006565biological_processL-serine catabolic process
A0008442molecular_function3-hydroxyisobutyrate dehydrogenase activity
A0009083biological_processbranched-chain amino acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046395biological_processcarboxylic acid catabolic process
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0051289biological_processprotein homotetramerization
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD A 299
ChainResidue
AILE7
AMSE64
ALEU65
APRO66
ATHR96
AVAL121
AGLY123
ALYS171
APHE239
ALYS246
AASP247
AGLY8
AHOH307
AHOH322
AHOH330
ALEU9
AGLY10
AHIS11
AMSE12
APHE30
AASP31
ALEU32

Functional Information from PROSITE/UniProt
site_idPS00895
Number of Residues14
Details3_HYDROXYISOBUT_DH 3-hydroxyisobutyrate dehydrogenase signature. FIGLGhMGapMAtN
ChainResidueDetails
APHE6-ASN19

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"22128181","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22128181","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-11-05

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