7A4U

Crystal structure of lid-truncated apo BiP in an oligomeric state

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	10
Details	binding site for residue GOL A 601

Chain	Residue
A	GLY36
A	HOH834
A	THR37
A	LYS96
A	GLU201
A	GLY227
A	GLY228
A	ASP231
A	GOL606
A	HOH726

---

site_id	AC2
Number of Residues	3
Details	binding site for residue GOL A 602

Chain	Residue
A	ASP178
A	GLN182
A	LYS185

---

site_id	AC3
Number of Residues	5
Details	binding site for residue GOL A 603

Chain	Residue
A	GLU498
A	GLU502
A	GLU514
A	HOH793
A	HOH797

---

site_id	AC4
Number of Residues	4
Details	binding site for residue GOL A 604

Chain	Residue
A	VAL419
A	ARG439
A	ASN440
A	HOH811

---

site_id	AC5
Number of Residues	4
Details	binding site for residue GOL A 605

Chain	Residue
A	ARG439
A	ASN440
A	HOH735
A	HOH839

---

site_id	AC6
Number of Residues	9
Details	binding site for residue GOL A 606

Chain	Residue
A	THR37
A	THR38
A	TYR39
A	GLY226
A	GLY227
A	ASP391
A	GOL601
A	HOH743
A	HOH784

---

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. VFDLGGGAfdvSLL

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	4
Details	BINDING: BINDING => ECO:0000269|PubMed:29064368, ECO:0000312|PDB:6EOE, ECO:0000312|PDB:6EOF

Chain	Residue	Details
A	GLY36
A	GLY227
A	GLU293
A	GLY364

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P11021

Chain	Residue	Details
A	LYS96

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06761

Chain	Residue	Details
A	SER86

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P20029

Chain	Residue	Details
A	LYS125
A	LYS213
A	LYS326

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029

Chain	Residue	Details
A	TYR160

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8

Chain	Residue	Details
A	LYS271

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029

Chain	Residue	Details
A	LYS353

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P20029

Chain	Residue	Details
A	LYS447

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P0DMV8

Chain	Residue	Details
A	ARG492

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphothreonine; alternate => ECO:0000250|UniProtKB:P11021

Chain	Residue	Details
A	THR518

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P11021

Chain	Residue	Details
A	LYS352

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P11021

Chain	Residue	Details
A	LYS353

---