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1UXU

Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Thermoproteus tenax

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008886molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity
A0008911molecular_functionlactaldehyde dehydrogenase (NAD+) activity
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 754
ChainResidue
AGLU249
AGLY255
AHOH2147
AHOH2148
AHOH2153
AHOH2159

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAP A 502
ChainResidue
APHE167
ALYS191
ASER193
AILE194
APRO223
AGLY224
AGLU228
APHE241
AGLY243
ASER244
AVAL247
AGLU395
APHE397
AHOH2275
AHOH2277
AHOH2278
AHOH2279
AHOH2285
AILE164
ATHR165
APRO166

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AMP A 503
ChainResidue
AARG72
AARG79
AILE133
AGLY134
AGLY135
APRO139
AASP141
ATRP142
AARG154
AARG155
AARG440
ATRP498
AHOH2115
AHOH2280
AHOH2281

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE G3H A 504
ChainResidue
AASN168
ATYR169
AARG296
ACYS297
AASP298
AARG454
AHIS455
AGLY456
AHOH2245
AHOH2283
AHOH2285
AHOH2286

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:15288789
ChainResidueDetails
AGLU263
ACYS297

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1UXR
ChainResidueDetails
AARG72
AARG79
ATYR184

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1UXU
ChainResidueDetails
AGLY134
AARG154
AASN168
AARG296
AHIS455

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11842090, ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1KY8, ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP, ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR, ECO:0007744|PDB:1UXU, ECO:0007744|PDB:1UXV
ChainResidueDetails
ATHR165
AGLY224
AGLU228
ASER244

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1UXT
ChainResidueDetails
ALYS191

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11842090, ECO:0000269|PubMed:15288789, ECO:0007744|PDB:1KY8, ECO:0007744|PDB:1UXN, ECO:0007744|PDB:1UXP, ECO:0007744|PDB:1UXQ, ECO:0007744|PDB:1UXR, ECO:0007744|PDB:1UXV
ChainResidueDetails
AGLY265
AGLU395

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4s
ChainResidueDetails
ACYS297
AGLU263
AASN168

223166

PDB entries from 2024-07-31

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