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3DRM

2.2 Angstrom Crystal Structure of Thr114Phe Alpha1-Antitrypsin

Functional Information from GO Data
ChainGOidnamespacecontents
A0002020molecular_functionprotease binding
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005794cellular_componentGolgi apparatus
A0006953biological_processacute-phase response
A0007596biological_processblood coagulation
A0030134cellular_componentCOPII-coated ER to Golgi transport vesicle
A0031093cellular_componentplatelet alpha granule lumen
A0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
A0042802molecular_functionidentical protein binding
A0043231cellular_componentintracellular membrane-bounded organelle
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. VKFNKPFVFlM
ChainResidueDetails
AVAL364-MET374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by Staphylococcus aureus aureolysin/Aur => ECO:0000269|PubMed:3533918
ChainResidueDetails
ALYS328

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by Staphylococcus aureus serine and cysteine proteinases => ECO:0000269|PubMed:3533918
ChainResidueDetails
ASER330

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Reactive bond
ChainResidueDetails
AMET358

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER14

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: S-cysteinyl cysteine
ChainResidueDetails
ACYS232

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER359

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320
ChainResidueDetails
AASN46

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169
ChainResidueDetails
AASN83

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320
ChainResidueDetails
AASN247

227111

PDB entries from 2024-11-06

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