1LGB

INTERACTION OF A LEGUME LECTIN WITH THE N2 FRAGMENT OF HUMAN LACTOTRANSFERRIN OR WITH THE ISOLATED BIANTENNARY GLYCOPEPTIDE: ROLE OF THE FUCOSE MOIETY

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0030246	molecular_function	carbohydrate binding
B	0005515	molecular_function	protein binding
B	0030246	molecular_function	carbohydrate binding
C	0005576	cellular_component	extracellular region

Functional Information from PDB Data

site_id	A
Number of Residues	6
Details	MANNOSE BINDING SITE

Chain	Residue
A	GLY99
A	ASP81
A	ASN125
B	GLY29
B	ALA30
B	GLU31

---

site_id	B
Number of Residues	2
Details	FUCOSE BINDING CAVITY

Chain	Residue
B	PHE32
B	GLU31

---

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
C	TYR92-GLY101

---

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

Chain	Residue	Details
C	TYR192-PHE208

---

site_id	PS00307
Number of Residues	7
Details	LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVEFDT

Chain	Residue	Details
A	VAL116-THR122

---

site_id	PS00308
Number of Residues	10
Details	LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. VPEWVRIGFS

Chain	Residue	Details
B	VAL16-SER25

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	30
Details	Peptide: {"description":"Kaliocin-1","featureId":"PRO_0000035733"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10089347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10828980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12450380","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16201406","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17543335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22900286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8371268","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8594202","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8703903","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8931543","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9003186","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5.","authors":["Vikram P.","Prem Kumar R.","Singh N.","Kumar J.","Ethayathulla A.S.","Sharma S.","Kaur P.","Singh T.P."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10089347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10828980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11128996","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12450380","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1581307","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16201406","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17543335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22900286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8371268","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8594202","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8931543","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9003186","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5.","authors":["Vikram P.","Prem Kumar R.","Singh N.","Kumar J.","Ethayathulla A.S.","Sharma S.","Kaur P.","Singh T.P."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Site: {"description":"Important for iron binding"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15299444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1581307","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16201406","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8069634","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5.","authors":["Vikram P.","Prem Kumar R.","Singh N.","Kumar J.","Ethayathulla A.S.","Sharma S.","Kaur P.","Singh T.P."]}}]}

Chain

Residue

Details

---