4FTG

The crystal structure of an AHNAK peptide in complex with the S100A10/AnxA2 heterotetramer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001765	biological_process	membrane raft assembly
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0006900	biological_process	vesicle budding from membrane
A	0008289	molecular_function	lipid binding
A	0009986	cellular_component	cell surface
A	0010756	biological_process	positive regulation of plasminogen activation
A	0016363	cellular_component	nuclear matrix
A	0031012	cellular_component	extracellular matrix
A	0042789	biological_process	mRNA transcription by RNA polymerase II
A	0042803	molecular_function	protein homodimerization activity
A	0043547	biological_process	positive regulation of GTPase activity
A	0044325	molecular_function	transmembrane transporter binding
A	0045121	cellular_component	membrane raft
A	0045921	biological_process	positive regulation of exocytosis
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0048306	molecular_function	calcium-dependent protein binding
A	0050767	biological_process	regulation of neurogenesis
A	0051496	biological_process	positive regulation of stress fiber assembly
A	0051894	biological_process	positive regulation of focal adhesion assembly
A	0070062	cellular_component	extracellular exosome
A	0072659	biological_process	protein localization to plasma membrane
A	0090575	cellular_component	RNA polymerase II transcription regulator complex
A	0098797	cellular_component	plasma membrane protein complex
A	1900026	biological_process	positive regulation of substrate adhesion-dependent cell spreading
A	1905686	biological_process	positive regulation of plasma membrane repair
A	1990665	cellular_component	AnxA2-p11 complex
B	0001765	biological_process	membrane raft assembly
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005886	cellular_component	plasma membrane
B	0006900	biological_process	vesicle budding from membrane
B	0008289	molecular_function	lipid binding
B	0009986	cellular_component	cell surface
B	0010756	biological_process	positive regulation of plasminogen activation
B	0016363	cellular_component	nuclear matrix
B	0031012	cellular_component	extracellular matrix
B	0042789	biological_process	mRNA transcription by RNA polymerase II
B	0042803	molecular_function	protein homodimerization activity
B	0043547	biological_process	positive regulation of GTPase activity
B	0044325	molecular_function	transmembrane transporter binding
B	0045121	cellular_component	membrane raft
B	0045921	biological_process	positive regulation of exocytosis
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0048306	molecular_function	calcium-dependent protein binding
B	0050767	biological_process	regulation of neurogenesis
B	0051496	biological_process	positive regulation of stress fiber assembly
B	0051894	biological_process	positive regulation of focal adhesion assembly
B	0070062	cellular_component	extracellular exosome
B	0072659	biological_process	protein localization to plasma membrane
B	0090575	cellular_component	RNA polymerase II transcription regulator complex
B	0098797	cellular_component	plasma membrane protein complex
B	1900026	biological_process	positive regulation of substrate adhesion-dependent cell spreading
B	1905686	biological_process	positive regulation of plasma membrane repair
B	1990665	cellular_component	AnxA2-p11 complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IPA A 101

Chain	Residue
A	PRO1
A	HIS6
A	ALA7
A	THR10
B	GLN3
B	HIS6
B	ALA7

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA B 101

Chain	Residue
B	GLU9
B	THR10
A	PRO1
B	HIS6

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA E 101

Chain	Residue
A	GLY77
E	LYS2
E	VAL3
E	THR4

---

Functional Information from PROSITE/UniProt

site_id	PS00303
Number of Residues	22
Details	S100_CABP S-100/ICaBP type calcium binding protein signature. IMkdLDqcrDgkvGFqSFfsLI

Chain	Residue	Details
A	ILE54-ILE75

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	22
Details	Region: {"description":"Ancestral calcium site"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Murray L.","Brunton V.G.","Frame M.C.","Bensaad K.","Vousden K.H."]}}]}

Chain

Residue

Details

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