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6HGM

Crystal structure of Alpha1-antichymotrypsin variant NewBG-III-allo: an allosterically controlled new binding globulin with an unprecedentedly high ligand release efficacy

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0006953biological_processacute-phase response
A0006954biological_processinflammatory response
A0019216biological_processregulation of lipid metabolic process
A0030277biological_processmaintenance of gastrointestinal epithelium
A0030414molecular_functionpeptidase inhibitor activity
A0031093cellular_componentplatelet alpha granule lumen
A0034774cellular_componentsecretory granule lumen
A0035578cellular_componentazurophil granule lumen
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 401
ChainResidue
AARG349
BMET378
BMET391
BSER392

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 402
ChainResidue
ALYS174
AASP175
ALYS356
AHOH785

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 403
ChainResidue
AASN70
ALEU73
ASER237
ALYS260
AHIS69

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 404
ChainResidue
AASP259
AGLU263
AEDO407
AHOH512
AHOH562
AHOH589

site_idAC5
Number of Residues7
Detailsbinding site for residue CA A 405
ChainResidue
AASN70
AASP257
AHOH616
AHOH790
AHOH796
AHOH802
AHOH806

site_idAC6
Number of Residues7
Detailsbinding site for residue CA A 406
ChainResidue
AGLU86
AHOH580
AHOH623
AHOH719
AHOH795
AHOH833
AHOH885

site_idAC7
Number of Residues8
Detailsbinding site for residue EDO A 407
ChainResidue
AGLU89
AASP259
ALYS260
AGLU263
ACA404
AHOH512
AHOH589
AHOH622

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO A 408
ChainResidue
AGLU89
AALA90
AHIS93
AARG129
AASP133
AHOH528
AHOH656

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. VRFNRPFLMiI
ChainResidueDetails
BVAL370-ILE380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsDNA_BIND:
ChainResidueDetails
ALYS212-LYS214

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Reactive bond
ChainResidueDetails
ALEU360

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN10
AASN163

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN70

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN83

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN104
AASN248

218853

PDB entries from 2024-04-24

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