3EHR

Crystal Structure of Human Osteoclast Stimulating Factor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001503	biological_process	ossification
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0007165	biological_process	signal transduction
A	0017124	molecular_function	SH3 domain binding
A	0034774	cellular_component	secretory granule lumen
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0001503	biological_process	ossification
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0007165	biological_process	signal transduction
B	0017124	molecular_function	SH3 domain binding
B	0034774	cellular_component	secretory granule lumen
B	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712

Chain	Residue	Details
A	SER2
B	SER2

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	THR200
B	THR200

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692

Chain	Residue	Details
A	SER202
B	SER202

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER213
B	SER213

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