7EQU

Crystal structure of the C-lobe of lactoferrin produced by limited proteolysis using pepsin at 2.74A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
B	0005576	cellular_component	extracellular region

Functional Information from PROSITE/UniProt

site_id	PS00205
Number of Residues	10
Details	TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YlAVAVVKKA

Chain	Residue	Details
A	TYR433-ALA442

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site_id	PS00206
Number of Residues	17
Details	TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YtGAFRCLaedvGDVAF

Chain	Residue	Details
A	TYR526-PHE542

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site_id	PS00207
Number of Residues	31
Details	TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. DFrLLClDgtrkp...VteaqsChlAvapnHaVV

Chain	Residue	Details
A	ASP568-VAL598

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:9398529, ECO:0007744|PDB:1BLF

Chain	Residue	Details
A	ASP395
A	TYR433
A	TYR526
A	HIS595
B	ASP395
B	TYR433
B	TYR526
B	HIS595

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741

Chain	Residue	Details
A	THR459
A	ARG463
A	ALA465
A	GLY466
B	THR459
B	ARG463
B	ALA465
B	GLY466

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site_id	SWS_FT_FI3
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9398529, ECO:0000269|DOI:10.1016/j.idairyj.2021.104999, ECO:0007744|PDB:1BLF

Chain	Residue	Details
A	ASN368
A	ASN476
B	ASN368
B	ASN476

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:9398529, ECO:0000269|DOI:10.1016/j.idairyj.2021.104999, ECO:0007744|PDB:1BLF

Chain	Residue	Details
A	ASN545
B	ASN545

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