6HA7

Crystal structure of the BiP NBD and MANF complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016887	molecular_function	ATP hydrolysis activity
B	0005524	molecular_function	ATP binding
B	0016887	molecular_function	ATP hydrolysis activity
C	0002014	biological_process	vasoconstriction of artery involved in ischemic response to lowering of systemic arterial blood pressure
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005783	cellular_component	endoplasmic reticulum
C	0005788	cellular_component	endoplasmic reticulum lumen
C	0006986	biological_process	response to unfolded protein
C	0008083	molecular_function	growth factor activity
C	0008289	molecular_function	lipid binding
C	0033018	cellular_component	sarcoplasmic reticulum lumen
C	0036500	biological_process	ATF6-mediated unfolded protein response
C	0048471	cellular_component	perinuclear region of cytoplasm
C	0120146	molecular_function	sulfatide binding
C	1905897	biological_process	regulation of response to endoplasmic reticulum stress
D	0002014	biological_process	vasoconstriction of artery involved in ischemic response to lowering of systemic arterial blood pressure
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005783	cellular_component	endoplasmic reticulum
D	0005788	cellular_component	endoplasmic reticulum lumen
D	0006986	biological_process	response to unfolded protein
D	0008083	molecular_function	growth factor activity
D	0008289	molecular_function	lipid binding
D	0033018	cellular_component	sarcoplasmic reticulum lumen
D	0036500	biological_process	ATF6-mediated unfolded protein response
D	0048471	cellular_component	perinuclear region of cytoplasm
D	0120146	molecular_function	sulfatide binding
D	1905897	biological_process	regulation of response to endoplasmic reticulum stress

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue EDO A 501

Chain	Residue
A	ASP34
A	GLY36
A	VAL394

---

site_id	AC2
Number of Residues	2
Details	binding site for residue EDO B 501

Chain	Residue
B	ASP34
B	GLY36

---

Functional Information from PROSITE/UniProt

site_id	PS00297
Number of Residues	8
Details	HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS

Chain	Residue	Details
A	ILE33-SER40

---

site_id	PS00329
Number of Residues	14
Details	HSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGTfdvSLL

Chain	Residue	Details
A	VAL222-LEU235

---

site_id	PS01036
Number of Residues	15
Details	HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ

Chain	Residue	Details
A	ILE359-GLN373

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	310
Details	Region: {"description":"Nucleotide-binding (NBD)","evidences":[{"source":"UniProtKB","id":"P11021","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29064368","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EOE","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6EOF","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P11021","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06761","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DMV8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P11021","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P11021","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	124
Details	Region: {"description":"Interacts with ERN1, EIF2AK3 and ATF6","evidences":[{"source":"UniProtKB","id":"P55145","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	86
Details	Region: {"description":"Interacts with HSPA5","evidences":[{"source":"PubMed","id":"30710085","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---