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

3JQD

Crystal structure of pteridine reductase 1 (PTR1) from Trypanosoma brucei in ternary complex with cofactor (NADP+) and inhibitor 2-amino-4-oxo-6-phenyl-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile (DX7)

Replaces:  3BMJ
Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
B0016491molecular_functionoxidoreductase activity
C0016491molecular_functionoxidoreductase activity
D0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NAP A 269
ChainResidue
AARG14
ATHR64
AASN93
AALA94
ASER95
ATHR126
ALEU159
ACYS160
ATYR174
ALYS178
APRO204
AILE15
AGLY205
AVAL206
ASER207
ALEU208
ADX7270
AHOH283
AHOH291
AHOH337
AHOH341
AHOH422
ATYR34
AHOH457
AHOH459
AHOH571
AHIS35
AASN36
ASER37
AALA61
AASP62
ALEU63

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE DX7 A 270
ChainResidue
AARG14
ASER95
APHE97
AASP161
ATYR174
AGLY205
APRO210
ANAP269
AHOH327
AHOH459
AHOH568

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 271
ChainResidue
ACSX168
AHOH469

site_idAC4
Number of Residues36
DetailsBINDING SITE FOR RESIDUE NAP B 269
ChainResidue
BARG14
BILE15
BTYR34
BHIS35
BASN36
BSER37
BALA61
BASP62
BLEU63
BTHR64
BASN93
BALA94
BSER95
BTHR126
BLEU159
BCYS160
BTYR174
BLYS178
BPRO204
BGLY205
BVAL206
BSER207
BLEU208
BDX7270
BHOH279
BHOH288
BHOH302
BHOH309
BHOH323
BHOH336
BHOH353
BHOH365
BHOH434
BHOH436
BHOH438
BHOH518

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DX7 B 270
ChainResidue
BARG14
BSER95
BPHE97
BASP161
BCSX168
BTYR174
BGLY205
BVAL206
BPRO210
BNAP269
BHOH438
BHOH443
BHOH501

site_idAC6
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAP C 269
ChainResidue
CSER37
CALA61
CASP62
CLEU63
CTHR64
CASN93
CALA94
CSER95
CTHR126
CLEU159
CCYS160
CTYR174
CLYS178
CPRO204
CGLY205
CVAL206
CSER207
CLEU208
CDX7270
CHOH279
CHOH281
CHOH289
CHOH337
CHOH362
CHOH383
CHOH389
CHOH401
CHOH526
CARG14
CILE15
CTYR34
CHIS35
CASN36

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DX7 C 270
ChainResidue
CARG14
CSER95
CPHE97
CASP161
CTYR174
CGLY205
CPRO210
CNAP269
CHOH389
CHOH444

site_idAC8
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAP D 269
ChainResidue
DARG14
DILE15
DTYR34
DHIS35
DASN36
DSER37
DALA61
DASP62
DLEU63
DTHR64
DASN93
DALA94
DSER95
DTHR126
DLEU159
DCYS160
DTYR174
DLYS178
DPRO204
DGLY205
DVAL206
DSER207
DLEU208
DDX7270
DHOH276
DHOH310
DHOH332
DHOH342
DHOH354
DHOH358
DHOH390
DHOH396
DHOH537

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DX7 D 270
ChainResidue
DARG14
DSER95
DPHE97
DASP161
DCSX168
DTYR174
DGLY205
DPRO210
DNAP269
DHOH336
DHOH354
DHOH451

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. DamvdqpcmaFslYNMGKHALvGLTqSAA
ChainResidueDetails
AASP161-ALA189

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
AASP165

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BPHE171
BLYS178

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CPHE171
CLYS178

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DPHE171
DLYS178

site_idCSA13
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ATYR174
ALYS178

site_idCSA14
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DTYR174
DLYS178

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BASP165

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CASP165

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DASP165

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ASER152
ATYR174
ALYS178

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BTYR174
BLYS178

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CTYR174
CLYS178

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DSER152
DTYR174
DLYS178

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
APHE171
ALYS178

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon