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4OR0

Crystal Structure of Bovine Serum Albumin in complex with naproxen

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0005504molecular_functionfatty acid binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0008289molecular_functionlipid binding
A0009267biological_processcellular response to starvation
A0015643molecular_functiontoxic substance binding
A0019825molecular_functionoxygen binding
A0030170molecular_functionpyridoxal phosphate binding
A0032991cellular_componentprotein-containing complex
A0046872molecular_functionmetal ion binding
A0051902biological_processnegative regulation of mitochondrial depolarization
A0072732biological_processcellular response to calcium ion starvation
A1903981molecular_functionenterobactin binding
B0003677molecular_functionDNA binding
B0005504molecular_functionfatty acid binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0008289molecular_functionlipid binding
B0009267biological_processcellular response to starvation
B0015643molecular_functiontoxic substance binding
B0019825molecular_functionoxygen binding
B0030170molecular_functionpyridoxal phosphate binding
B0032991cellular_componentprotein-containing complex
B0046872molecular_functionmetal ion binding
B0051902biological_processnegative regulation of mitochondrial depolarization
B0072732biological_processcellular response to calcium ion starvation
B1903981molecular_functionenterobactin binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NPS A 601
ChainResidue
AASN390
AARG409
ATYR410
ALYS413
AVAL432
AGLY433
ALEU452
ASER488

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NPS A 602
ChainResidue
AARG208
AALA209
ALEU346
ALYS350
ASER479
ALEU480
AVAL481
APHE205

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NPS A 603
ChainResidue
AARG194
ALEU197
AARG198
ASER201
ATRP213
AARG217
ASER343
ALEU454
ALEU480

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PGE A 604
ChainResidue
APHE506
APHE550
ATHR578

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 605
ChainResidue
ATYR149
ALEU237
AHIS241
AARG256

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NPS B 601
ChainResidue
BASN390
BCYS391
BARG409
BTYR410
BLYS413
BTHR448
BSER488

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NPS B 602
ChainResidue
BARG208
BLEU326
BLEU346
BLYS350
BSER479
BLEU480
BVAL481
BNPS603

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NPS B 603
ChainResidue
BARG194
BLEU197
BARG198
BSER201
BALA209
BTRP213
BARG217
BLEU480
BNPS602

Functional Information from PROSITE/UniProt
site_idPS00212
Number of Residues25
DetailsALBUMIN_1 Albumin domain signature. YngvfqeCCqaEdkgaCLlpkietM
ChainResidueDetails
ATYR160-MET184
ATYR352-LEU376
APHE550-LEU574

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P02770
ChainResidueDetails
AHIS3
BHIS3

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22677715, ECO:0007744|PDB:3V03
ChainResidueDetails
AGLU6
BGLU6

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:22677715, ECO:0000269|PubMed:23769932, ECO:0007744|PDB:3V03, ECO:0007744|PDB:4JK4
ChainResidueDetails
AASP13
BASP258
AGLU243
AGLU251
AASP254
AASP258
BASP13
BGLU243
BGLU251
BASP254

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P02768
ChainResidueDetails
AHIS67
AHIS246
AASP248
BHIS67
BHIS246
BASP248

site_idSWS_FT_FI5
Number of Residues10
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02768
ChainResidueDetails
ASER5
BSER488
ASER58
ASER65
ASER418
ASER488
BSER5
BSER58
BSER65
BSER418

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P02768
ChainResidueDetails
ATHR83
ATHR419
ATHR421
BTHR83
BTHR419
BTHR421

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724
ChainResidueDetails
ALYS204
ALYS563
BLYS204
BLYS563

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724
ChainResidueDetails
ASER272
BSER272

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P02768
ChainResidueDetails
ALYS533
BLYS533

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P02770
ChainResidueDetails
ATHR545
BTHR545

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:21565706
ChainResidueDetails
ALYS127
BLYS127

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PDB entries from 2024-10-30

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