Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1RFV

Crystal structure of pyridoxal kinase complexed with ADP

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
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008478molecular_functionpyridoxal kinase activity
B0009443biological_processpyridoxal 5'-phosphate salvage
B0016301molecular_functionkinase activity
B0042816biological_processvitamin B6 metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AGLN119
AADP401

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN B 1402
ChainResidue
BADP1401

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ADP A 401
ChainResidue
ALYS225
AVAL226
AALA228
ATHR233
APHE237
ALEU267
AZN402
AHOH404
AHOH434
AGLN119
AASN150
ATHR186
ASER187
AMET223
AHIS224

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP B 1401
ChainResidue
BASP118
BASN150
BTHR186
BSER187
BMET223
BHIS224
BLYS225
BVAL226
BALA228
BTHR233
BPHE237
BMET263
BLEU267
BZN1402
BHOH1403
BHOH1414
BHOH1421
BHOH1440

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O00764
ChainResidueDetails
AASP235
BASP235

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1RFT
ChainResidueDetails
ASER12
ATHR47
AASP235
BSER12
BTHR47
BASP235

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR, ECO:0007744|PDB:1RFT
ChainResidueDetails
AASP113
ATHR148
ATHR186
BASP113
BTHR148
BTHR186

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1RFU
ChainResidueDetails
ATYR127
AGLY232
BTYR127
BGLY232

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR
ChainResidueDetails
AASN150
BASN150

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0007744|PDB:1LHR
ChainResidueDetails
AMET223
ATHR233
BMET223
BTHR233

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:10395444
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O00764
ChainResidueDetails
ASER59
ASER164
ASER213
ASER285
BSER59
BSER164
BSER213
BSER285

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

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
BGLY234
BTHR233
BGLY232
BASP235

231029

PDB entries from 2025-02-05

PDB statisticsPDBj update infoContact PDBjnumon