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3NRB

Crystal structure of a formyltetrahydrofolate deformylase (purU, PP_1943) from PSEUDOMONAS PUTIDA KT2440 at 2.05 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0006730biological_processone-carbon metabolic process
A0008864molecular_functionformyltetrahydrofolate deformylase activity
A0009058biological_processbiosynthetic process
A0016787molecular_functionhydrolase activity
B0006164biological_processpurine nucleotide biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0006730biological_processone-carbon metabolic process
B0008864molecular_functionformyltetrahydrofolate deformylase activity
B0009058biological_processbiosynthetic process
B0016787molecular_functionhydrolase activity
C0006164biological_processpurine nucleotide biosynthetic process
C0006189biological_process'de novo' IMP biosynthetic process
C0006730biological_processone-carbon metabolic process
C0008864molecular_functionformyltetrahydrofolate deformylase activity
C0009058biological_processbiosynthetic process
C0016787molecular_functionhydrolase activity
D0006164biological_processpurine nucleotide biosynthetic process
D0006189biological_process'de novo' IMP biosynthetic process
D0006730biological_processone-carbon metabolic process
D0008864molecular_functionformyltetrahydrofolate deformylase activity
D0009058biological_processbiosynthetic process
D0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 287
ChainResidue
AARG244
AASP249
AHOH375
AHOH524
AHOH564
CHOH307

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FLC A 289
ChainResidue
ALYS204
APRO205
ATYR206
AHIS207
AVAL251
AHOH352
AHOH487
APHE97
AMSE174
AHIS194

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 290
ChainResidue
APRO83
AARG84
ALEU270
AASP272
AHOH409
AHOH735

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD A 291
ChainResidue
AASN123
AHIS124
AMSE174
AGLN175
AHOH311

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 287
ChainResidue
BGLU112
BHOH348
BHOH349
DARG255

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 288
ChainResidue
BLYS74
BGLN155
BHOH313
BHOH375

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 289
ChainResidue
BARG82
BPRO83
BASP86
BLYS88

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD B 290
ChainResidue
BASN123
BHIS124
BMSE174
BGLN175
BHOH323

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA C 287
ChainResidue
CLYS96
CASP98
CALA128
CLEU129
CHOH322
CHOH573

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 288
ChainResidue
AASN30
CSER154
CLYS157
CHOH402

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD C 289
ChainResidue
CASN123
CHIS124
CMSE174
CGLN175
CHOH358

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA D 287
ChainResidue
BHOH451
DARG244
DASP249
DHOH371
DHOH382
DHOH752

site_idBC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FLC D 289
ChainResidue
DPHE97
DARG172
DHIS194
DLYS204
DPRO205
DTYR206
DHIS207
DVAL251
DHOH332
DHOH379

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO D 290
ChainResidue
DARG82
DPRO83
DLEU270
DASP272
DHOH325
DHOH358

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO D 291
ChainResidue
CHOH382
DPRO198
DLYS201

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD D 292
ChainResidue
DASN123
DHIS124
DMSE174
DGLN175
DHOH364
DHOH714

221051

PDB entries from 2024-06-12

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