1D5S

CRYSTAL STRUCTURE OF CLEAVED ANTITRYPSIN POLYMER

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005615	cellular_component	extracellular space

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	VAL364-MET374

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Reactive bond

Chain	Residue	Details
B	ARG358

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
B	SER359

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: S-cysteinyl cysteine

Chain	Residue	Details
A	CYS232

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site_id	SWS_FT_FI4
Number of Residues	1
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

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site_id	SWS_FT_FI5
Number of Residues	1
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

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site_id	SWS_FT_FI6
Number of Residues	1
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

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