1HSE

H253M N TERMINAL LOBE OF HUMAN LACTOFERRIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 400

Chain	Residue
A	ASP60
A	TYR92
A	TYR192
A	MET253
A	CO3401

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CO3 A 401

Chain	Residue
A	ASP60
A	TYR92
A	THR117
A	ARG121
A	THR122
A	ALA123
A	GLY124
A	TYR192
A	FE400

---

site_id	S1
Number of Residues	10
Details	METAL AND ANION BINDING SITE.

Chain	Residue
A	ASP60
A	CO3401
A	TYR92
A	THR117
A	ARG121
A	ALA123
A	GLY124
A	TYR192
A	MET253
A	FE400

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TYR92-GLY101

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

Chain	Residue	Details
A	TYR192-PHE208

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:12535064

Chain	Residue	Details
A	LYS73

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:12535064

Chain	Residue	Details
A	SER259

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72

Chain	Residue	Details
A	ASP60
A	TYR92
A	TYR192
A	MET253

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72

Chain	Residue	Details
A	THR117
A	ARG121
A	ALA123
A	GLY124

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Interaction with PspA

Chain	Residue	Details
A	ARG4
A	GLN13

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Important for iron binding

Chain	Residue	Details
A	ARG210

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site_id	SWS_FT_FI7
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15299444, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:8069634, ECO:0000269|Ref.72

Chain	Residue	Details
A	ASN137

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