2IBG

Crystal Structure of Hedgehog Bound to the FNIII Domains of Ihog

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0007267	biological_process	cell-cell signaling
E	0007275	biological_process	multicellular organism development
F	0007267	biological_process	cell-cell signaling
F	0007275	biological_process	multicellular organism development
G	0007267	biological_process	cell-cell signaling
G	0007275	biological_process	multicellular organism development
H	0007267	biological_process	cell-cell signaling
H	0007275	biological_process	multicellular organism development

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 401

Chain	Residue
B	HOH138
B	HOH146
B	HOH161
B	ASN526
B	SER532
B	PHE533
B	THR534
B	ALA629
B	THR630

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 C 402

Chain	Residue
C	HOH182
C	HOH187
C	HOH191
C	ASN526
C	SER532
C	PHE533
C	THR534
C	ALA629
C	THR630

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 403

Chain	Residue
A	HOH37
A	HOH70
A	ASN526
A	SER532
A	PHE533
A	THR534
A	ALA629
A	THR630

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 404

Chain	Residue
A	ARG503
A	VAL505
A	ARG547
E	ASP191
E	HIS193

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 405

Chain	Residue
D	ARG503
D	VAL505
D	LYS509
D	ARG547
H	ASP191
H	HIS193

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 406

Chain	Residue
B	ARG503
B	GLY506
B	ARG547
B	LYS567

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 407

Chain	Residue
C	ARG503
C	VAL505
C	LYS509
C	ARG547
G	ASP191

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 E 408

Chain	Residue
E	ARG161
E	LYS165

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 H 409

Chain	Residue
H	ARG161
H	LYS165
H	HOH348

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 410

Chain	Residue
F	GLY179
F	ARG181
G	ARG142
H	GLY179
H	ARG181

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 E 411

Chain	Residue
E	MET174
E	GLY179
E	ARG181
F	MET174
G	GLY179
G	ARG181

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 412

Chain	Residue
E	HIS194
E	HOH305
E	HOH313
E	HOH315

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	424
Details	Domain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	380
Details	Domain: {"description":"Fibronectin type-III 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17077139","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q15465","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---