1NGI

STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT

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 CA A 489

Chain	Residue
A	GLU175
A	ASP199
A	HOH666
A	HOH668
A	HOH670
A	HOH671
A	HOH673

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site_id	AC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE ANP A 486

Chain	Residue
A	THR14
A	TYR15
A	GLY201
A	GLY202
A	GLY203
A	THR204
A	GLY230
A	GLU268
A	LYS271
A	ARG272
A	SER275
A	GLY338
A	GLY339
A	SER340
A	ARG342
A	ILE343
A	ASP366
A	HOH529
A	HOH557
A	HOH564
A	HOH572
A	HOH666
A	HOH667
A	HOH668
A	HOH670
A	HOH674
A	GLY12
A	THR13

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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

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

Chain	Residue	Details
A	ILE197-LEU210

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

Chain	Residue	Details
A	ILE334-LYS348

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	GLY12
A	LYS71

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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

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

Chain	Residue	Details
A	LYS319

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Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS71

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 656

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

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