5F1X

Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ATP

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	binding site for residue ATP A 501

Chain	Residue
A	GLY36
A	GLU293
A	LYS296
A	ARG297
A	SER300
A	GLY363
A	GLY364
A	SER365
A	ARG367
A	ASP391
A	HOH601
A	THR37
A	HOH637
A	HOH662
A	HOH673
A	HOH693
A	HOH701
A	HOH751
A	HOH754
A	THR38
A	TYR39
A	GLY226
A	GLY227
A	GLY228
A	THR229
A	GLY255

---

site_id	AC2
Number of Residues	27
Details	binding site for residue ATP B 501

Chain	Residue
B	GLY36
B	THR37
B	THR38
B	TYR39
B	GLY226
B	GLY227
B	GLY228
B	THR229
B	GLY255
B	GLU293
B	LYS296
B	ARG297
B	SER300
B	GLY363
B	GLY364
B	SER365
B	ARG367
B	ILE368
B	ASP391
B	HOH602
B	HOH624
B	HOH641
B	HOH647
B	HOH650
B	HOH677
B	HOH699
B	HOH714

---

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":"PubMed","id":"28286085","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21526763","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06761","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
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_FI5
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_FI6
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_FI7
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_FI8
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---