2QWQ

Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP hydrolyzed form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 488

Chain	Residue
A	GLY12
A	THR13
A	LYS71
A	GLU175
A	THR204
A	ADP487
A	HOH3180

---

site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ADP A 487

Chain	Residue
A	TYR15
A	GLY201
A	GLY202
A	GLY230
A	GLU268
A	LYS271
A	ARG272
A	SER275
A	GLY338
A	GLY339
A	SER340
A	ARG342
A	ILE343
A	ASP366
A	PO4488
A	GOL3148
A	HOH3180
A	HOH3209
A	THR13
A	THR14

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY A 1022

Chain	Residue
A	ASN31
A	ASP32
A	LYS126
A	ILE130

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 3147

Chain	Residue
A	THR13
A	LYS71
A	ARG72
A	TYR149
A	PHE150
A	THR204
A	THR226

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 3148

Chain	Residue
A	TYR15
A	LYS56
A	GLU231
A	ASP234
A	GLU268
A	ADP487

---

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	ILE9-SER16

---

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

Chain	Residue	Details
A	ILE197-LEU210

---

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

Chain	Residue	Details
A	ILE334-LYS348

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	GLY12
A	LYS71

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: BINDING => ECO:0007744|PDB:2QWL, ECO:0007744|PDB:2QWM, ECO:0007744|PDB:2QWN, ECO:0007744|PDB:2QWO, ECO:0007744|PDB:2QWP, ECO:0007744|PDB:2QWQ

Chain	Residue	Details
A	THR14
A	TYR15
A	GLY202
A	GLU268
A	LYS271
A	SER275
A	GLY339

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P11142

Chain	Residue	Details
A	SER2

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P63017

Chain	Residue	Details
A	LYS108
A	LYS328

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11142

Chain	Residue	Details
A	SER153
A	SER329
A	SER362

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P11142

Chain	Residue	Details
A	LYS246

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P63017

Chain	Residue	Details
A	LYS319

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1kaz

Chain	Residue	Details
A	LYS71

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 656

Chain	Residue	Details
A	ASP10
A	LYS71	enhance reactivity
A	GLU175
A	ASP199

---