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PDB code:
Information on 2nad
PDB:
2nad
Compound:
Nad-dependent formate dehydrogenase (holo form) co
Classification:
OXIDOREDUCTASE(ALDEHYDE(D),NAD+(A))
Entry date in PDB:
1995-01-26
Resolution [Å]:
2.00
R-Factor:
0.114
CHAIN:
A
SWISS-PROT/TREMBL:
P33160
KEYWORD:
3D-structure NAD Oxidoreductase
EC:
1.2.1.2
SCOP:
c.2.1.4
Alpha and beta proteins (a/b)
NAD(P)-binding Rossmann-fold domains
NAD(P)-binding Rossmann-fold domains
Formate/glycerate dehydrogenases, NAD-domain
Formate dehydrogenase
Pseudomonas sp., strain 101
SCOP:
c.23.12.1
Alpha and beta proteins (a/b)
Flavodoxin-like
Formate/glycerate dehydrogenase catalytic domain-like
Formate/glycerate dehydrogenases, substrate-binding domain
Formate dehydrogenase
Pseudomonas sp., strain 101
SCOP:
c.23.12.1
Alpha and beta proteins (a/b)
Flavodoxin-like
Formate/glycerate dehydrogenase catalytic domain-like
Formate/glycerate dehydrogenases, substrate-binding domain
Formate dehydrogenase
Pseudomonas sp., strain 101
GO:
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
L-serine biosynthesis
CHAIN:
B
SWISS-PROT/TREMBL:
P33160
KEYWORD:
3D-structure NAD Oxidoreductase
EC:
1.2.1.2
SCOP:
c.2.1.4
Alpha and beta proteins (a/b)
NAD(P)-binding Rossmann-fold domains
NAD(P)-binding Rossmann-fold domains
Formate/glycerate dehydrogenases, NAD-domain
Formate dehydrogenase
Pseudomonas sp., strain 101
SCOP:
c.23.12.1
Alpha and beta proteins (a/b)
Flavodoxin-like
Formate/glycerate dehydrogenase catalytic domain-like
Formate/glycerate dehydrogenases, substrate-binding domain
Formate dehydrogenase
Pseudomonas sp., strain 101
SCOP:
c.23.12.1
Alpha and beta proteins (a/b)
Flavodoxin-like
Formate/glycerate dehydrogenase catalytic domain-like
Formate/glycerate dehydrogenases, substrate-binding domain
Formate dehydrogenase
Pseudomonas sp., strain 101
GO:
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
L-serine biosynthesis
Image Source:
PDB
Homologous structures to 2nad classified in ArchDB
2nac
A - percentage of sequence identity: 100