1E7H

HUMAN SERUM ALBUMIN COMPLEXED WITH HEXADECANOIC ACID (PALMITIC ACID)

> Summary

Summary for 1E7H

Related1AO6 1BJ5 1BKE 1BM0 1E78 1E7A 1E7B 1E7C 1E7E 1E7F 1E7G 1E7I 1UOR
DescriptorSERUM ALBUMIN
Functional Keywordsplasma protein, metal-binding, lipid-binding
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationSecreted P02768
Total number of polymer chains1
Total molecular weight68366.81
Authors
Bhattacharya, A.A.,Gruene, T.,Curry, S. (deposition date: 2000-08-29, release date: 2000-12-08, modification date: 2009-02-24)
Primary citation
Bhattacharya, A.A.,Grune, T.,Curry, S.
Crystallographic Analysis Reveals Common Modes of Binding of Medium and Long-Chain Fatty Acids to Human Serum Albumin
J.Mol.Biol., 303:721-, 2000
PubMed: 11061971
DOI: 10.1006/JMBI.2000.4158
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.43 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers201.6%11.6%2.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 1e7h
no rotation
Molmil generated image of 1e7h
rotated about x axis by 90°
Molmil generated image of 1e7h
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
ASERUM ALBUMINpolymer58566571.81
UniProt (P02768)
Pfam (PF00273)
HOMO SAPIENS (HUMAN)@PDBj
PALMITIC ACIDnon-polymer256.47
waterwater18.029

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight66571.8
Non-Polymers*Number of molecules7
Total molecular weight1795.0
All*Total molecular weight68366.8
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2.43 Å)
Cell axes190.09038.75095.870
Cell angles90.00104.9690.00
SpacegroupC 1 2 1
Resolution limits12.00 - 2.43
the highest resolution shell value2.540 - 2.430
R-factor0.214
R-work0.21400
the highest resolution shell value0.334
R-free0.27200
the highest resolution shell value0.337
RMSD bond length0.006
RMSD bond angle1.200 (24.600*)

Data Collection Statistics

Resolution limits11.99 - 2.44
the highest resolution shell value -
Number of reflections24122
Rmerge_l_obs0.046
the highest resolution shell value0.178
Completeness92.9
the highest resolution shell value87.8*
Redundancy2.7
the highest resolution shell value2.7
I/sigma(I)0

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1Vapor diffusion, sitting drop*7K*

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein100 (mg/ml)
21reservoirPEG335025-30 (%(w/v))
31reservoirpotassium phosphate50 (mM)
Annotated Information is extracted from Literature Info*
Curry, S., (1998) Nature Struct. Biol., 5, 827.

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005604cellular_componentbasement membrane
A0072562cellular_componentblood microparticle
A0005783cellular_componentendoplasmic reticulum
A0070062cellular_componentextracellular exosome
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005794cellular_componentGolgi apparatus
A0043209cellular_componentmyelin sheath
A0005634cellular_componentnucleus
A0031093cellular_componentplatelet alpha granule lumen
A0043234cellular_componentprotein complex
A0016209molecular_functionantioxidant activity
A0051087molecular_functionchaperone binding
A0005507molecular_functioncopper ion binding
A0003677molecular_functionDNA binding
A0008144molecular_functiondrug binding
A0005504molecular_functionfatty acid binding
A0042802molecular_functionidentical protein binding
A0030170molecular_functionpyridoxal phosphate binding
A0015643molecular_functiontoxic substance binding
A0008270molecular_functionzinc ion binding
A0015721biological_processbile acid and bile salt transport
A0008206biological_processbile acid metabolic process
A0007596biological_processblood coagulation
A0098869biological_processcellular oxidant detoxification
A0009267biological_processcellular response to starvation
A0019836biological_processhemolysis by symbiont of host erythrocytes
A0042157biological_processlipoprotein metabolic process
A0051659biological_processmaintenance of mitochondrion location
A0043066biological_processnegative regulation of apoptotic process
A0043069biological_processnegative regulation of programmed cell death
A0030168biological_processplatelet activation
A0002576biological_processplatelet degranulation
A0046010biological_processpositive regulation of circadian sleep/wake cycle, non-REM sleep
A0006898biological_processreceptor-mediated endocytosis
A0046689biological_processresponse to mercury ion
A0007584biological_processresponse to nutrient
A0010033biological_processresponse to organic substance
A0070541biological_processresponse to platinum ion
A0001895biological_processretina homeostasis
A0044281biological_processsmall molecule metabolic process
A0043252biological_processsodium-independent organic anion transport
A0055085biological_processtransmembrane transport
A0006810biological_processtransport
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC15BINDING SITE FOR RESIDUE PLM A1001
ChainResidue
AARG117
ALEU135
ATYR138
ATYR161
AHOH

AC28BINDING SITE FOR RESIDUE PLM A1002
ChainResidue
AVAL46
ALEU69
ATYR150
ALEU251
AALA254
AARG257
ALEU283
ASER287

AC38BINDING SITE FOR RESIDUE PLM A1003
ChainResidue
ASER342
AVAL344
AARG348
AASN391
AGLY434
ALEU453
AARG485
APLM

AC411BINDING SITE FOR RESIDUE PLM A1004
ChainResidue
ALEU387
ATYR411
ALEU457
ALEU460
ALEU463
AHIS464
ASER489
APLM
AHOH
AHOH
AHOH

AC58BINDING SITE FOR RESIDUE PLM A1005
ChainResidue
ATYR401
APHE502
APHE507
ALYS525
AALA528
AHIS535
AMET548
AGLN580

AC63BINDING SITE FOR RESIDUE PLM A1006
ChainResidue
AARG209
AALA210
ALYS351

AC72BINDING SITE FOR RESIDUE PLM A1007
ChainResidue
AARG218
AARG222

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
PLM_1e7h_A_100219PALMITIC ACID binding site
ChainResidueligand
AVAL7PLM: PALMITIC ACID
AARG10PLM: PALMITIC ACID
ALEU14PLM: PALMITIC ACID
APHE19PLM: PALMITIC ACID
ALEU22-VAL23PLM: PALMITIC ACID
AVAL46PLM: PALMITIC ACID
ALEU66PLM: PALMITIC ACID
ALEU69-PHE70PLM: PALMITIC ACID
ATYR150PLM: PALMITIC ACID
APRO152PLM: PALMITIC ACID
ALEU251PLM: PALMITIC ACID
AALA254PLM: PALMITIC ACID
AARG257-ALA258PLM: PALMITIC ACID
ALEU283-LEU284PLM: PALMITIC ACID
ASER287PLM: PALMITIC ACID

PLM_1e7h_A_100111PALMITIC ACID binding site
ChainResidueligand
ALEU115PLM: PALMITIC ACID
AARG117PLM: PALMITIC ACID
AMET123PLM: PALMITIC ACID
ALEU135PLM: PALMITIC ACID
ATYR138-LEU139PLM: PALMITIC ACID
AALA158PLM: PALMITIC ACID
ATYR161PLM: PALMITIC ACID
APHE165PLM: PALMITIC ACID
ALEU182PLM: PALMITIC ACID
AARG186PLM: PALMITIC ACID

PLM_1e7h_A_100618PALMITIC ACID binding site
ChainResidueligand
AARG209-ALA210PLM: PALMITIC ACID
ALYS212-ALA213PLM: PALMITIC ACID
AVAL216PLM: PALMITIC ACID
APHE228PLM: PALMITIC ACID
ASER232PLM: PALMITIC ACID
AASP324-VAL325PLM: PALMITIC ACID
ALEU327-GLY328PLM: PALMITIC ACID
ALEU331PLM: PALMITIC ACID
ALEU347PLM: PALMITIC ACID
AALA350-LYS351PLM: PALMITIC ACID
AGLU354PLM: PALMITIC ACID
ASER480PLM: PALMITIC ACID
AVAL482PLM: PALMITIC ACID

PLM_1e7h_A_100713PALMITIC ACID binding site
ChainResidueligand
AARG218-LEU219PLM: PALMITIC ACID
AARG222-PHE223PLM: PALMITIC ACID
ALEU238PLM: PALMITIC ACID
AVAL241-HIS242PLM: PALMITIC ACID
AARG257PLM: PALMITIC ACID
ALEU260PLM: PALMITIC ACID
AILE264PLM: PALMITIC ACID
ASER287PLM: PALMITIC ACID
AILE290-ALA291PLM: PALMITIC ACID

PLM_1e7h_A_100324PALMITIC ACID binding site
ChainResidueligand
ASER342PLM: PALMITIC ACID
AVAL344-LEU345PLM: PALMITIC ACID
AARG348PLM: PALMITIC ACID
APRO384PLM: PALMITIC ACID
ALEU387-ILE388PLM: PALMITIC ACID
AASN391-CYS392PLM: PALMITIC ACID
APHE403PLM: PALMITIC ACID
ALEU407PLM: PALMITIC ACID
AARG410-TYR411PLM: PALMITIC ACID
ALEU430PLM: PALMITIC ACID
AVAL433-GLY434PLM: PALMITIC ACID
ACYS437-CYS438PLM: PALMITIC ACID
AMET446PLM: PALMITIC ACID
AALA449-GLU450PLM: PALMITIC ACID
ALEU453PLM: PALMITIC ACID
AARG485-PRO486PLM: PALMITIC ACID

PLM_1e7h_A_100420PALMITIC ACID binding site
ChainResidueligand
ALEU387PLM: PALMITIC ACID
AARG410-TYR411PLM: PALMITIC ACID
ALYS414-VAL415PLM: PALMITIC ACID
AVAL418PLM: PALMITIC ACID
ATHR422-LEU423PLM: PALMITIC ACID
AVAL426PLM: PALMITIC ACID
ALEU430PLM: PALMITIC ACID
ALEU453PLM: PALMITIC ACID
ALEU457PLM: PALMITIC ACID
ALEU460PLM: PALMITIC ACID
ALEU463-HIS464PLM: PALMITIC ACID
AVAL473PLM: PALMITIC ACID
AARG485PLM: PALMITIC ACID
APHE488-SER489PLM: PALMITIC ACID
ALEU491PLM: PALMITIC ACID

PLM_1e7h_A_100519PALMITIC ACID binding site
ChainResidueligand
ATYR401PLM: PALMITIC ACID
AASN405PLM: PALMITIC ACID
APHE502PLM: PALMITIC ACID
APHE507PLM: PALMITIC ACID
APHE509PLM: PALMITIC ACID
ALYS525PLM: PALMITIC ACID
AALA528-LEU529PLM: PALMITIC ACID
ALEU532PLM: PALMITIC ACID
AHIS535PLM: PALMITIC ACID
AVAL547-MET548PLM: PALMITIC ACID
APHE551-ALA552PLM: PALMITIC ACID
ALEU575-VAL576PLM: PALMITIC ACID
ASER579-GLN580PLM: PALMITIC ACID
ALEU583PLM: PALMITIC ACID

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
PS002123Albumin domain signature. [FY]-x(6)-C-C-x(2)-{C}-x(4)-C-[LFY]-x(6)-[LIVMFYW]
ChainResidueDetails
ANA*
ANA*
ANA*

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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI31Bilirubin.
ChainResidueDetails
ALYS240

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Catalytic Information from CSA

site_idNumber of ResiduesDetails
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Catalytic Information from CATRES

site_idNumber of ResiduesDetails

> Sequence Neighbor

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