6LOS

Crystal structure of mouse PEDF in complex with heterotrimeric collagen model peptide.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001822	biological_process	kidney development
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005576	cellular_component	extracellular region
A	0005604	cellular_component	basement membrane
A	0005615	cellular_component	extracellular space
A	0007614	biological_process	short-term memory
A	0010447	biological_process	response to acidic pH
A	0010596	biological_process	negative regulation of endothelial cell migration
A	0010629	biological_process	negative regulation of gene expression
A	0010976	biological_process	positive regulation of neuron projection development
A	0016525	biological_process	negative regulation of angiogenesis
A	0030424	cellular_component	axon
A	0042470	cellular_component	melanosome
A	0042698	biological_process	ovulation cycle
A	0043025	cellular_component	neuronal cell body
A	0043203	cellular_component	axon hillock
A	0046685	biological_process	response to arsenic-containing substance
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050769	biological_process	positive regulation of neurogenesis
A	0060041	biological_process	retina development in camera-type eye
A	0060767	biological_process	epithelial cell proliferation involved in prostate gland development
A	0060770	biological_process	negative regulation of epithelial cell proliferation involved in prostate gland development
A	0071279	biological_process	cellular response to cobalt ion
A	0071300	biological_process	cellular response to retinoic acid
A	0071333	biological_process	cellular response to glucose stimulus
A	0071549	biological_process	cellular response to dexamethasone stimulus
A	1901652	biological_process	response to peptide

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue SO4 A 501

Chain	Residue
A	ARG251
A	LEU304
A	LYS305
A	THR306

---

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 502

Chain	Residue
A	THR163
A	ARG164
A	TRP182
A	GLN186

---

site_id	AC3
Number of Residues	6
Details	binding site for residue SO4 A 503

Chain	Residue
A	SER151
A	SER152
A	HOH612
F	HIS17
H	LYS12
A	LYS150

---

Functional Information from PROSITE/UniProt

site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. YHLNQPFLFvL

Chain	Residue	Details
A	TYR387-LEU397

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---