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- PDB-8api: THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICAT... -

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Entry
Database: PDB / ID: 8api
TitleTHE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM
Components(ALPHA-1 ANTITRYPSIN (CHAIN ...) x 2
KeywordsPROTEINASE INHIBITOR
Function / homology
Function and homology information


Cargo concentration in the ER / COPII-mediated vesicle transport / COPII-coated ER to Golgi transport vesicle / endoplasmic reticulum-Golgi intermediate compartment membrane / platelet alpha granule lumen / acute-phase response / Post-translational protein phosphorylation / serine-type endopeptidase inhibitor activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / blood coagulation ...Cargo concentration in the ER / COPII-mediated vesicle transport / COPII-coated ER to Golgi transport vesicle / endoplasmic reticulum-Golgi intermediate compartment membrane / platelet alpha granule lumen / acute-phase response / Post-translational protein phosphorylation / serine-type endopeptidase inhibitor activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / blood coagulation / Platelet degranulation / collagen-containing extracellular matrix / protease binding / ficolin-1-rich granule lumen / endoplasmic reticulum lumen / intracellular membrane-bounded organelle / Neutrophil degranulation / Golgi apparatus / endoplasmic reticulum / extracellular space / extracellular exosome / extracellular region / identical protein binding
Similarity search - Function
Antithrombin; Chain I, domain 2 / Antithrombin, subunit I, domain 2 / Alpha-1-antitrypsin; domain 1 / Alpha-1-antitrypsin, domain 1 / Serpin, conserved site / Serpins signature. / Serpin superfamily, domain 2 / Serpin family / Serpin domain / Serpin superfamily ...Antithrombin; Chain I, domain 2 / Antithrombin, subunit I, domain 2 / Alpha-1-antitrypsin; domain 1 / Alpha-1-antitrypsin, domain 1 / Serpin, conserved site / Serpins signature. / Serpin superfamily, domain 2 / Serpin family / Serpin domain / Serpin superfamily / Serpin superfamily, domain 1 / Serpin (serine protease inhibitor) / SERine Proteinase INhibitors / Roll / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
CYSTEINE / Alpha-1-antitrypsin
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / Resolution: 3.1 Å
AuthorsLoebermann, H. / Tokuoka, R. / Deisenhofer, J. / Huber, R.
Citation
Journal: Protein Eng. / Year: 1989
Title: The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism.
Authors: Engh, R. / Lobermann, H. / Schneider, M. / Wiegand, G. / Huber, R. / Laurell, C.B.
#1: Journal: J.Mol.Biol. / Year: 1984
Title: Human Alpha1-Proteinase Inhibitor. Crystal Structure Analysis of Two Crystal Modifications, Molecular Model and Preliminary Analysis of the Implications for Function
Authors: Loebermann, H. / Tokuoka, R. / Deisenhofer, J. / Huber, R.
#2: Journal: Hoppe-Seyler's Z.Physiol.Chem. / Year: 1982
Title: Interaction of Human Alpha1-Proteinase Inhibitor with Chymotrypsinogena and Crystallization of a Proteolytically Modified Alpha1-Proteinase Inhibitor
Authors: Loebermann, H. / Lottspeich, F. / Bode, W. / Huber, R.
#3: Journal: J.Biol.Chem. / Year: 1982
Title: The Biosynthesis of Rat Alpha1-Antitrypsin
Authors: Carlson, J. / Stenflo, J.
#4: Journal: FEBS Lett. / Year: 1981
Title: Human Alpha1-Antitrypsin. Carbohydrate Attachment and Sequence Homology
Authors: Carrell, R.W. / Jeppsson, J.-O. / Vaughan, L. / Brennan, S.O. / Owen, M.C. / Boswell, D.R.
#5: Journal: J.Biol.Chem. / Year: 1980
Title: Studies on the Oligosaccharide Chains of Human Alpha1-Protease Inhibitor. II. Structure of Oligosaccharides
Authors: Mega, T. / Lujan, E. / Yoshida, A.
History
DepositionSep 8, 1988Processing site: BNL
SupersessionOct 15, 1990ID: 6API
Revision 1.0Oct 15, 1990Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / pdbx_validate_chiral / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_database_status.process_site / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 10, 2024Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ALPHA-1 ANTITRYPSIN (CHAIN A)
B: ALPHA-1 ANTITRYPSIN (CHAIN B)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,3386
Polymers43,2542
Non-polymers2,0844
Water2,864159
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7340 Å2
ΔGint-12 kcal/mol
Surface area17550 Å2
MethodPISA
Unit cell
Length a, b, c (Å)119.700, 119.700, 216.300
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number179
Space group name H-MP6522
Atom site foot note1: RESIDUE PRO B 361 IS A CIS PROLINE.
2: AN OCCUPANCY AND B VALUE OF 0.0 INDICATES THAT NO SIGNIFICANT ELECTRON DENSITY WAS FOUND IN THE FINAL FOURIER MAP.

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Components

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ALPHA-1 ANTITRYPSIN (CHAIN ... , 2 types, 2 molecules AB

#1: Protein ALPHA-1 ANTITRYPSIN (CHAIN A)


Mass: 39114.320 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P01009
#2: Protein/peptide ALPHA-1 ANTITRYPSIN (CHAIN B)


Mass: 4139.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P01009

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Sugars , 2 types, 3 molecules

#3: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1114.016 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-2DManpa1-6[DManpa1-3]DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2-2-1/a4-b1_b4-c1_c3-d1_c6-e1_e2-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(2+1)][b-D-GlcpNAc]{}}}}}}LINUCSPDB-CARE
#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE

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Non-polymers , 2 types, 160 molecules

#5: Chemical ChemComp-CYS / CYSTEINE / Cysteine


Type: L-peptide linking / Mass: 121.158 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H7NO2S
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 159 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsIN THIS ENTRY CHAIN IDENTIFIER *C* IS USED FOR A CYSTEINE RESIDUE WHICH FORMS A DISULFIDE BOND WITH ...IN THIS ENTRY CHAIN IDENTIFIER *C* IS USED FOR A CYSTEINE RESIDUE WHICH FORMS A DISULFIDE BOND WITH CYS A 232. SEE REFERENCE 1 FOR FURTHER DISCUSSION ON THE POSSIBLE ROLE OF CYS A 232 IN THE PROPOSED STRUCTURE FOR THE ACTIVE INHIBITOR.
Nonpolymer detailsTHE CARBOHYDRATE CHAINS PRESENTED AT THE END OF THIS ENTRY ARE NOT COMPLETE. SOME OF THE SUGAR ...THE CARBOHYDRATE CHAINS PRESENTED AT THE END OF THIS ENTRY ARE NOT COMPLETE. SOME OF THE SUGAR RESIDUES COULD NOT BE LOCATED IN THE ELECTRON DENSITY MAPS.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 5.17 Å3/Da / Density % sol: 76.21 %
Crystal grow
*PLUS
Temperature: 4 ℃ / pH: 8 / Method: vapor diffusion
Details: Loebermann, H., (1982) Hoppe-Seyler'S Z.Physiol. Chem., 363, 1377.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
12.8 Msodium potassium phosphate1reservoir
25 mMsodium phosphate1drop
36-7 mg/mlprotein1drop

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Data collection

Reflection
*PLUS
Highest resolution: 3.1 Å / Num. obs: 15607 / % possible obs: 90 % / Biso Wilson estimate: 276 Å2
Reflection shell
*PLUS
Num. possible: 62

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Processing

SoftwareName: EREF / Classification: refinement
RefinementRfactor Rwork: 0.215 / Highest resolution: 3.1 Å
Details: AN OCCUPANCY AND B VALUE OF 0.0 INDICATES THAT NO SIGNIFICANT ELECTRON DENSITY WAS FOUND IN THE FINAL FOURIER MAP. ATOMS WITH THERMAL FACTORS WHICH CALCULATE LESS THAN 6.00 ARE ASSIGNED THIS ...Details: AN OCCUPANCY AND B VALUE OF 0.0 INDICATES THAT NO SIGNIFICANT ELECTRON DENSITY WAS FOUND IN THE FINAL FOURIER MAP. ATOMS WITH THERMAL FACTORS WHICH CALCULATE LESS THAN 6.00 ARE ASSIGNED THIS VALUE. THIS IS THE LOWEST VALUE ALLOWED BY THE REFINEMENT PROGRAM.
Refinement stepCycle: LAST / Highest resolution: 3.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2989 0 138 159 3286
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.013
X-RAY DIFFRACTIONo_bond_d_na
X-RAY DIFFRACTIONo_bond_d_prot
X-RAY DIFFRACTIONo_angle_d
X-RAY DIFFRACTIONo_angle_d_na
X-RAY DIFFRACTIONo_angle_d_prot
X-RAY DIFFRACTIONo_angle_deg2.4
X-RAY DIFFRACTIONo_angle_deg_na
X-RAY DIFFRACTIONo_angle_deg_prot
X-RAY DIFFRACTIONo_dihedral_angle_d
X-RAY DIFFRACTIONo_dihedral_angle_d_na
X-RAY DIFFRACTIONo_dihedral_angle_d_prot
X-RAY DIFFRACTIONo_improper_angle_d
X-RAY DIFFRACTIONo_improper_angle_d_na
X-RAY DIFFRACTIONo_improper_angle_d_prot
X-RAY DIFFRACTIONo_mcbond_it
X-RAY DIFFRACTIONo_mcangle_it
X-RAY DIFFRACTIONo_scbond_it
X-RAY DIFFRACTIONo_scangle_it
Refinement
*PLUS
Highest resolution: 3.1 Å / Lowest resolution: 9999 Å / Num. reflection obs: 15607 / Rfactor obs: 0.215
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Type: o_angle_d

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