3D48

Crystal structure of a prolactin receptor antagonist bound to the extracellular domain of the prolactin receptor

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0001937	biological_process	negative regulation of endothelial cell proliferation
P	0005148	molecular_function	prolactin receptor binding
P	0005179	molecular_function	hormone activity
P	0005515	molecular_function	protein binding
P	0005576	cellular_component	extracellular region
P	0005615	cellular_component	extracellular space
P	0007166	biological_process	cell surface receptor signaling pathway
P	0007565	biological_process	female pregnancy
P	0007595	biological_process	lactation
P	0016525	biological_process	negative regulation of angiogenesis
P	0030879	biological_process	mammary gland development
P	0031667	biological_process	response to nutrient levels
P	0031904	cellular_component	endosome lumen
P	0038161	biological_process	prolactin signaling pathway
P	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
P	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
P	1902895	biological_process	positive regulation of miRNA transcription
P	1903489	biological_process	positive regulation of lactation
R	0004896	molecular_function	cytokine receptor activity
R	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO3 P 1

Chain	Residue
P	SER57
P	CYS58
P	HIS59
P	LEU171
P	CYS174

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CO3 R 211

Chain	Residue
R	TYR190
R	TRP191

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CO3 R 212

Chain	Residue
R	GLN102
R	CYS12
R	ARG13

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO3 R 213

Chain	Residue
R	THR39
R	TYR40
R	HIS41
R	ILE76
R	MET78

---

Functional Information from PROSITE/UniProt

site_id	PS01352
Number of Residues	78
Details	HEMATOPO_REC_L_F1 Long hematopoietin receptor, single chain family signature. LwIkWspptlidlktgwftllYEIrlkpekaaeweihfagqqtefkils..LhpgqkylvqvRcKpdhgy....WsaWspatfI

Chain	Residue	Details
R	LEU123-ILE200

---

site_id	PS00266
Number of Residues	34
Details	SOMATOTROPIN_1 Somatotropin, prolactin and related hormones signature 1. ChTssLaTPedkeqAqqmnqkdFlslivsIlrSW

Chain	Residue	Details
P	CYS58-TRP91

---

site_id	PS00338
Number of Residues	18
Details	SOMATOTROPIN_2 Somatotropin, prolactin and related hormones signature 2. CLRrDShKIDnYlkLlkC

Chain	Residue	Details
P	CYS174-CYS191

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01239","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15687336","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	101
Details	Domain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Motif: {"description":"WSXWS motif"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---