PDB ID : 1gad [A4]

Color

ARa IRb





 a AR:All Residues
 b IR:Interface Residues

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Secondary Structure


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Slab plane

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Chain
Chain name Ribbon Spacefill Cαonly
OLIGAMI PDB
AO
BP
CO
DP
Title
COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY

Structure Summary
PDB ID Mutant OPM Pub Med Method/Resolution HETNAM
1gad
8636984 X-RAY DIFFRACTION/1.8 NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE
Chain Formula
Amino Acid sequence SCOPe Family Level CATH Homology Level
[A4] [A4] [A4]

Structual Classification
SCOPe
SCOPe ID Chain Class Fold Superfamily Family Protein Domain Species
29950 O:0-148
O:313-330		Alpha and beta proteins (a/b)NAD(P)-binding Rossmann-fold domainsNAD(P)-binding Rossmann-fold domainsGlyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domainGlyceraldehyde-3-phosphate dehydrogenase (GAPDH)Escherichia coli [TaxId: 562]
39865 O:149-312Alpha and beta proteins (a+b)FwdE/GAPDH domain-likeGlyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domainGAPDH-likeGlyceraldehyde-3-phosphate dehydrogenase (GAPDH)Escherichia coli [TaxId: 562]
29951 P:0-148
P:313-330		Alpha and beta proteins (a/b)NAD(P)-binding Rossmann-fold domainsNAD(P)-binding Rossmann-fold domainsGlyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domainGlyceraldehyde-3-phosphate dehydrogenase (GAPDH)Escherichia coli [TaxId: 562]
39866 P:149-312Alpha and beta proteins (a+b)FwdE/GAPDH domain-likeGlyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domainGAPDH-likeGlyceraldehyde-3-phosphate dehydrogenase (GAPDH)Escherichia coli [TaxId: 562]

CATH
CATH ID Node Class Architecture Topology Homology
1gadO013.40.50.720:3-Layer(aba) Sandwich:Rossmann fold:NAD(P)-binding Rossmann-like Domain
1gadO023.30.360.10:2-Layer Sandwich:Dihydrodipicolinate Reductase; domain 2:Dihydrodipicolinate Reductase; domain 2
1gadP013.40.50.720:3-Layer(aba) Sandwich:Rossmann fold:NAD(P)-binding Rossmann-like Domain
1gadP023.30.360.10:2-Layer Sandwich:Dihydrodipicolinate Reductase; domain 2:Dihydrodipicolinate Reductase; domain 2