Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1UXP

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 A1504
ChainResidue
AGLU249
AGLY255
AHOH2159
AHOH2166
AHOH2175
AHOH2177

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AMP A1502
ChainResidue
AGLY134
AGLY135
ATYR137
APRO139
AASP141
ATRP142
AARG154
AARG155
AARG440
ATRP498
AHOH2117
AHOH2118
AHOH2327
AARG72
AARG79
AILE133

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAP A1503
ChainResidue
AILE164
ATHR165
APRO166
APHE167
AASN168
ALYS191
ASER193
AILE194
APRO223
AGLY224
AALA227
AGLU228
APHE241
ATHR242
AGLY243
ASER244
AVAL247
AGLU263
ALEU264
AGLY265
AGLY266
ACYS297
AGLU395
APHE397
ALEU423
AHOH2328
AHOH2329
AHOH2330
AHOH2331

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

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon