Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3DRU

Crystal Structure of Gly117Phe Alpha1-Antitrypsin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002020	molecular_function	protease binding
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005794	cellular_component	Golgi apparatus
A	0006953	biological_process	acute-phase response
A	0007596	biological_process	blood coagulation
A	0007599	biological_process	hemostasis
A	0030134	cellular_component	COPII-coated ER to Golgi transport vesicle
A	0030414	molecular_function	peptidase inhibitor activity
A	0031012	cellular_component	extracellular matrix
A	0031093	cellular_component	platelet alpha granule lumen
A	0033116	cellular_component	endoplasmic reticulum-Golgi intermediate compartment membrane
A	0042802	molecular_function	identical protein binding
A	0070062	cellular_component	extracellular exosome
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0002020	molecular_function	protease binding
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005794	cellular_component	Golgi apparatus
B	0006953	biological_process	acute-phase response
B	0007596	biological_process	blood coagulation
B	0007599	biological_process	hemostasis
B	0030134	cellular_component	COPII-coated ER to Golgi transport vesicle
B	0030414	molecular_function	peptidase inhibitor activity
B	0031012	cellular_component	extracellular matrix
B	0031093	cellular_component	platelet alpha granule lumen
B	0033116	cellular_component	endoplasmic reticulum-Golgi intermediate compartment membrane
B	0042802	molecular_function	identical protein binding
B	0070062	cellular_component	extracellular exosome
B	1904813	cellular_component	ficolin-1-rich granule lumen
C	0002020	molecular_function	protease binding
C	0004867	molecular_function	serine-type endopeptidase inhibitor activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005783	cellular_component	endoplasmic reticulum
C	0005788	cellular_component	endoplasmic reticulum lumen
C	0005794	cellular_component	Golgi apparatus
C	0006953	biological_process	acute-phase response
C	0007596	biological_process	blood coagulation
C	0007599	biological_process	hemostasis
C	0030134	cellular_component	COPII-coated ER to Golgi transport vesicle
C	0030414	molecular_function	peptidase inhibitor activity
C	0031012	cellular_component	extracellular matrix
C	0031093	cellular_component	platelet alpha granule lumen
C	0033116	cellular_component	endoplasmic reticulum-Golgi intermediate compartment membrane
C	0042802	molecular_function	identical protein binding
C	0070062	cellular_component	extracellular exosome
C	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PROSITE/UniProt

site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. VKFNKPFVFlM

Chain	Residue	Details
A	VAL364-MET374

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	SITE: (Microbial infection) Cleavage; by Staphylococcus aureus aureolysin/Aur => ECO:0000269\|PubMed:3533918

Chain	Residue	Details
A	LYS328
B	LYS328
C	LYS328

site_id	SWS_FT_FI2
Number of Residues	3
Details	SITE: (Microbial infection) Cleavage; by Staphylococcus aureus serine and cysteine proteinases => ECO:0000269\|PubMed:3533918

Chain	Residue	Details
A	SER330
B	SER330
C	SER330

site_id	SWS_FT_FI3
Number of Residues	3
Details	SITE: Reactive bond

Chain	Residue	Details
A	MET358
B	MET358
C	MET358

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269\|PubMed:26091039

Chain	Residue	Details
A	SER14
B	SER14
C	SER14

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: S-cysteinyl cysteine

Chain	Residue	Details
A	CYS232
B	CYS232
C	CYS232

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER359
B	SER359
C	SER359

site_id	SWS_FT_FI7
Number of Residues	3
Details	CARBOHYD: 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

Chain	Residue	Details
A	ASN46
B	ASN46
C	ASN46

site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: 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

Chain	Residue	Details
A	ASN83
B	ASN83
C	ASN83

site_id	SWS_FT_FI9
Number of Residues	3
Details	CARBOHYD: 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

Chain	Residue	Details
A	ASN247
B	ASN247
C	ASN247

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)