4Z1I

Crystal structure of human Trap1 with AMPPNP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0005524	molecular_function	ATP binding
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0005524	molecular_function	ATP binding
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0005524	molecular_function	ATP binding
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue ANP A 801

Chain	Residue
A	GLU115
A	SER180
A	GLY199
A	GLN200
A	PHE201
A	GLY202
A	VAL203
A	GLY204
A	PHE205
A	THR251
A	ARG402
A	ASN119
A	MG802
A	ALA123
A	LYS126
A	ASP158
A	MET163
A	ASN171
A	SER178
A	GLY179

---

site_id	AC2
Number of Residues	2
Details	binding site for residue MG A 802

Chain	Residue
A	ASN119
A	ANP801

---

site_id	AC3
Number of Residues	2
Details	binding site for residue MG B 802

Chain	Residue
B	ASN119
B	ANP801

---

site_id	AC4
Number of Residues	2
Details	binding site for residue MG C 802

Chain	Residue
C	ASN119
C	ANP801

---

site_id	AC5
Number of Residues	2
Details	binding site for residue MG D 802

Chain	Residue
D	ASN119
D	ANP801

---

site_id	AC6
Number of Residues	24
Details	binding site for Di-peptide ANP B 801 and ASN B 119

Chain	Residue
B	GLU115
B	LEU116
B	ILE117
B	SER118
B	ALA120
B	SER121
B	ASP122
B	ALA123
B	ASP158
B	MET163
B	ASN171
B	SER178
B	GLY179
B	SER180
B	GLY199
B	GLN200
B	PHE201
B	GLY202
B	VAL203
B	GLY204
B	PHE205
B	THR251
B	ARG402
B	MG802

---

site_id	AC7
Number of Residues	25
Details	binding site for Di-peptide ANP B 801 and ARG B 402

Chain	Residue
B	ARG114
B	GLU115
B	ASN119
B	ALA123
B	ASP158
B	MET163
B	ASN171
B	SER178
B	GLY179
B	SER180
B	ILE198
B	GLY199
B	GLN200
B	PHE201
B	GLY202
B	VAL203
B	GLY204
B	PHE205
B	THR251
B	ASN399
B	LEU400
B	SER401
B	GLU403
B	LEU404
B	MG802

---

site_id	AC8
Number of Residues	27
Details	binding site for Di-peptide ANP C 801 and ASN C 119

Chain	Residue
C	GLY204
C	PHE205
C	THR251
C	ARG402
C	MG802
C	GLU115
C	LEU116
C	ILE117
C	SER118
C	ALA120
C	SER121
C	ASP122
C	ALA123
C	LYS126
C	ASP158
C	MET163
C	ASN171
C	LEU172
C	ARG177
C	SER178
C	GLY179
C	SER180
C	GLY199
C	GLN200
C	PHE201
C	GLY202
C	VAL203

---

site_id	AC9
Number of Residues	26
Details	binding site for Di-peptide ANP D 801 and ARG D 402

Chain	Residue
D	ARG114
D	GLU115
D	ASN119
D	ALA123
D	LYS126
D	ASP158
D	MET163
D	ASN171
D	SER178
D	GLY179
D	SER180
D	ILE198
D	GLY199
D	GLN200
D	PHE201
D	GLY202
D	VAL203
D	GLY204
D	PHE205
D	THR251
D	ASN399
D	LEU400
D	SER401
D	GLU403
D	LEU404
D	MG802

---

site_id	AD1
Number of Residues	25
Details	binding site for Di-peptide ANP D 801 and ASN D 119

Chain	Residue
D	GLU115
D	LEU116
D	ILE117
D	SER118
D	ALA120
D	SER121
D	ASP122
D	ALA123
D	LYS126
D	ASP158
D	MET163
D	ASN171
D	SER178
D	GLY179
D	SER180
D	GLY199
D	GLN200
D	PHE201
D	GLY202
D	VAL203
D	GLY204
D	PHE205
D	THR251
D	ARG402
D	MG802

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASN119
B	ARG402
C	ASN119
C	ASP158
C	ASN171
C	PHE205
C	ARG402
D	ASN119
D	ASP158
D	ASN171
D	PHE205
A	ASP158
D	ARG402
A	ASN171
A	PHE205
A	ARG402
B	ASN119
B	ASP158
B	ASN171
B	PHE205

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5XHZ0

Chain	Residue	Details
A	SER170
B	SER170
C	SER170
D	SER170

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q5XHZ0

Chain	Residue	Details
A	THR174
B	THR174
C	THR174
D	THR174

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER194
B	SER194
C	SER194
D	SER194

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CQN1

Chain	Residue	Details
A	LYS262
D	LYS262
D	LYS324
D	LYS431
A	LYS324
A	LYS431
B	LYS262
B	LYS324
B	LYS431
C	LYS262
C	LYS324
C	LYS431

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS332
D	LYS332
D	LYS424
D	LYS466
A	LYS424
A	LYS466
B	LYS332
B	LYS424
B	LYS466
C	LYS332
C	LYS424
C	LYS466

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	THR494
B	THR494
C	THR494
D	THR494

---