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1VFE

HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY SER (R121S)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 400
ChainResidue
AASP60
ATYR92
ATYR192
AHIS253
ACO3401

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CO3 A 401
ChainResidue
AASP60
ATYR92
ATHR117
ASER121
ATHR122
AALA123
ATYR192
AHIS253
AFE400

site_idBST
Number of Residues10
DetailsMETAL AND ANION BINDING SITE.
ChainResidue
AASP60
ACO3401
ATYR92
ATHR117
ASER121
AALA123
AGLY124
ATYR192
AHIS253
AFE400

Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
ChainResidueDetails
ATYR92-GLY101

site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLrdgaGDVAF
ChainResidueDetails
ATYR192-PHE208

site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLCpDntrkp...VdkfkdChlArvpsHaVV
ChainResidueDetails
AGLU226-VAL256

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsPeptide: {"description":"Kaliocin-1","featureId":"PRO_0000035733"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsPeptide: {"description":"Lactoferroxin-A","featureId":"PRO_0000035734"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsRegion: {"description":"Interaction with lipopolysaccharide"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsRegion: {"description":"Interaction with PspA"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsRegion: {"description":"Involved in glycosaminoglycan binding"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"12535064","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12535064","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding 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."]}}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsBinding 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."]}}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsSite: {"description":"Interaction with PspA"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsSite: {"description":"Important for iron binding"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"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."]}}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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