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1RFT

Crystal structure of pyridoxal kinase complexed with AMP-PCP and pyridoxamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008478molecular_functionpyridoxal kinase activity
A0009443biological_processpyridoxal 5'-phosphate salvage
A0016301molecular_functionkinase activity
A0042816biological_processvitamin B6 metabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
AACP401

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 404
ChainResidue
AASP113
ATHR148
ATHR186
AACP401
AHOH417

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ACP A 401
ChainResidue
ASER187
AMET223
ALYS225
AVAL226
AALA228
ATHR233
AGLY234
APHE237
ALEU267
AZN403
AK404
AHOH409
ATYR127
AASN150
ATHR186

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PXM A 402
ChainResidue
ASER12
AVAL19
AHIS46
ATHR47
ATYR84
AVAL231
AASP235
AHOH433

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O00764
ChainResidueDetails
AASP235

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1RFT
ChainResidueDetails
ASER12
ATHR47
AASP235

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR, ECO:0007744|PDB:1RFT
ChainResidueDetails
AASP113
ATHR148
ATHR186

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1RFU
ChainResidueDetails
ATYR127
AGLY232

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR
ChainResidueDetails
AASN150

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0007744|PDB:1LHR
ChainResidueDetails
AMET223
ATHR233

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:10395444
ChainResidueDetails
AMET1

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O00764
ChainResidueDetails
ASER59
ASER164
ASER213
ASER285

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
AGLY234
ATHR233
AGLY232
AASP235

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PDB entries from 2024-07-17

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