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2I1O

Crystal Structure of a Nicotinate Phosphoribosyltransferase from Thermoplasma acidophilum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004514molecular_functionnicotinate-nucleotide diphosphorylase (carboxylating) activity
A0004516molecular_functionnicotinate phosphoribosyltransferase activity
A0009435biological_processNAD biosynthetic process
A0016740molecular_functiontransferase activity
A0016763molecular_functionpentosyltransferase activity
A0016874molecular_functionligase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
AARG24
ATHR25
AMET180
ATHR197

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 502
ChainResidue
AHOH870
ATYR21
AHIS182
ALEU210
AASP237
AMPD401

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 503
ChainResidue
APRO47
AGLY118
ALYS299
APHE301
AHOH919

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 504
ChainResidue
AARG243
APHE246
AHOH862

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 505
ChainResidue
ACYS333
AHIS334

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 506
ChainResidue
AARG329
ATHR331
AHIS334
AGLU370
ATYR387
AHOH865
AHOH887

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 701
ChainResidue
ACYS330
ACYS333
ACYS350

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 702
ChainResidue
ACYS330
ACYS348
ACYS350
AGLY351
AHOH904

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A 601
ChainResidue
AARG142
AGLY271
AGLY272
ALEU273
AGLY290
AGLY292
ATHR293

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 401
ChainResidue
ATYR21
APHE138
ATHR179
AARG235
APO4502
AHOH819

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 402
ChainResidue
APHE136
AVAL177
ALYS206
ATYR233
AMET268

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY A 552
ChainResidue
AASP68
AHIS364

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:15753098
ChainResidueDetails
ATYR21
APHE138
ASER240

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:15753098, ECO:0007744|PDB:1YTK
ChainResidueDetails
ATHR179
AARG235
AGLY272
ATHR293

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.3
ChainResidueDetails
ACYS330
ACYS333
ACYS348
ACYS350

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphohistidine => ECO:0000250|UniProtKB:P22253
ChainResidueDetails
AHIS182

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PDB entries from 2024-05-29

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