1QJM

Crystal Structure of a Complex of Lactoferrin with a Lanthanide Ion (SM3+) at 3.4 Angstrom Resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001503	biological_process	ossification
A	0001817	biological_process	regulation of cytokine production
A	0002227	biological_process	innate immune response in mucosa
A	0002376	biological_process	immune system process
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005769	cellular_component	early endosome
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0006811	biological_process	monoatomic ion transport
A	0006826	biological_process	iron ion transport
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0016787	molecular_function	hydrolase activity
A	0019731	biological_process	antibacterial humoral response
A	0019732	biological_process	antifungal humoral response
A	0031665	biological_process	negative regulation of lipopolysaccharide-mediated signaling pathway
A	0032680	biological_process	regulation of tumor necrosis factor production
A	0033690	biological_process	positive regulation of osteoblast proliferation
A	0042581	cellular_component	specific granule
A	0043066	biological_process	negative regulation of apoptotic process
A	0045669	biological_process	positive regulation of osteoblast differentiation
A	0046872	molecular_function	metal ion binding
A	0051241	biological_process	negative regulation of multicellular organismal process
A	0055037	cellular_component	recycling endosome
A	0060349	biological_process	bone morphogenesis
A	1900159	biological_process	positive regulation of bone mineralization involved in bone maturation
A	1900229	biological_process	negative regulation of single-species biofilm formation in or on host organism
A	1902732	biological_process	positive regulation of chondrocyte proliferation
A	2000308	biological_process	negative regulation of tumor necrosis factor (ligand) superfamily member 11 production
A	2001205	biological_process	negative regulation of osteoclast development

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SM A 690

Chain	Residue
A	ASP60
A	TYR92
A	TYR192
A	HIS253
A	CO3692

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SM A 691

Chain	Residue
A	HIS595
A	CO3693
A	ASP395
A	TYR433
A	ARG463
A	TYR526

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CO3 A 692

Chain	Residue
A	ASP60
A	TYR92
A	ARG121
A	SER122
A	ALA123
A	GLY124
A	SM690

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CO3 A 693

Chain	Residue
A	ASP395
A	TYR433
A	THR459
A	ARG463
A	THR464
A	ALA465
A	ALA466
A	SM691

---

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
A	TYR433-SER442

---

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

Chain	Residue	Details
A	TYR192-PHE208
A	TYR526-PHE542

---

site_id	PS00207
Number of Residues	31
Details	TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. KYeLLCpDntrkp...VdafkeChlArvpsHaVV

Chain	Residue	Details
A	LYS226-VAL256
A	ASP568-VAL598

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	327
Details	Domain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	329
Details	Domain: {"description":"Transferrin-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10366507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531474","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11599026","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of Lactoferrin with 6-(Hydroxymethyl)oxane-2,3,4,5-tetrol at 3.49 A resolution.","authors":["Mir R.","Kaur A.","Singh A.K.","Singh N.","Kaur P.","Sharma S.","Singh T.P."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10366507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531475","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of Lactoferrin with 6-(Hydroxymethyl)oxane-2,3,4,5-tetrol at 3.49 A resolution.","authors":["Mir R.","Kaur A.","Singh A.K.","Singh N.","Kaur P.","Sharma S.","Singh T.P."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---