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1P33

Pteridine reductase from Leishmania tarentolae complex with NADPH and MTX

Functional Information from GO Data
ChainGOidnamespacecontents
A0006729biological_processtetrahydrobiopterin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0031427biological_processresponse to methotrexate
A0047040molecular_functionpteridine reductase activity
B0006729biological_processtetrahydrobiopterin biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0031427biological_processresponse to methotrexate
B0047040molecular_functionpteridine reductase activity
C0006729biological_processtetrahydrobiopterin biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0031427biological_processresponse to methotrexate
C0047040molecular_functionpteridine reductase activity
D0006729biological_processtetrahydrobiopterin biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0031427biological_processresponse to methotrexate
D0047040molecular_functionpteridine reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NDP A 300
ChainResidue
AGLY13
ASER67
AASN109
AALA110
ASER111
ASER112
AASP142
AMET179
AVAL180
AASP181
ATYR194
AARG17
ALYS198
APRO224
AGLY225
ALEU226
ASER227
AMTX351
AHOH400
AHOH473
AHOH541
ALEU18
AHIS38
AARG39
ASER40
AALA64
AASP65
ALEU66

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NDP B 301
ChainResidue
BGLY13
BLYS16
BARG17
BLEU18
BHIS36
BHIS38
BARG39
BSER40
BALA64
BASP65
BLEU66
BSER67
BASN109
BALA110
BSER111
BSER112
BASP142
BMET179
BVAL180
BTYR194
BLYS198
BPRO224
BGLY225
BSER227
BVAL228
BMTX352
BHOH412

site_idAC3
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NDP C 302
ChainResidue
CGLY13
CALA15
CARG17
CLEU18
CTYR37
CHIS38
CARG39
CSER40
CASP65
CLEU66
CSER67
CASN109
CALA110
CSER111
CSER112
CASP142
CSER146
CMET179
CVAL180
CTYR194
CLYS198
CPRO224
CGLY225
CLEU226
CSER227
CVAL228
CMTX353

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NDP D 303
ChainResidue
DLYS198
DPRO224
DGLY225
DSER227
DVAL228
DMTX354
DHOH428
DGLY13
DALA15
DARG17
DLEU18
DHIS38
DARG39
DSER40
DLEU66
DSER67
DASN109
DALA110
DSER111
DSER112
DASP142
DMET179
DVAL180
DTYR194

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MTX A 351
ChainResidue
AARG17
ASER111
APHE113
APRO115
AASP181
ALEU188
ATYR191
ATYR194
ALEU226
ALEU229
APRO230
ATYR241
ANDP300
AHOH484

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MTX B 352
ChainResidue
BARG17
BSER111
BPHE113
BPRO115
BASP181
BLEU188
BTYR191
BTYR194
BLEU226
BPRO230
BMET233
BTYR241
BNDP301

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MTX C 353
ChainResidue
CARG17
CSER111
CPHE113
CPRO115
CASP181
CLEU188
CTYR191
CTYR194
CLEU226
CLEU229
CPRO230
CMET233
CTYR241
CNDP302

site_idAC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MTX D 354
ChainResidue
DARG17
DSER111
DPHE113
DPRO115
DASP181
DTYR191
DTYR194
DLEU229
DPRO230
DMET233
DTYR241
DNDP303
DHOH509

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. DamtsqpllgYtmYTMAKEALeGLTrSAA
ChainResidueDetails
AASP181-ALA209

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR194
BTYR194
CTYR194
DTYR194

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12925782
ChainResidueDetails
CGLY13
CTYR194
DGLY13
DTYR194
AGLY13
ATYR194
BGLY13
BTYR194

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER175
BSER175
CSER175
DSER175

218500

PDB entries from 2024-04-17

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