6DLU

Cryo-EM of the GMPPCP-bound human dynamin-1 polymer assembled on the membrane in the constricted state

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
P	0003924	molecular_function	GTPase activity
P	0005525	molecular_function	GTP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	binding site for residue GCP B 801

Chain	Residue
B	GLN40
B	THR65
B	GLY139
B	LYS206
B	ASP208
B	LEU209
B	VAL235
B	ASN236
B	ARG237
B	SER238
B	GLN239
B	SER41
B	ILE242
B	MG802
P	ASP211
B	GLY43
B	LYS44
B	SER45
B	SER46
B	ARG59
B	GLY60
B	VAL64

---

site_id	AC2
Number of Residues	3
Details	binding site for residue MG B 802

Chain	Residue
B	SER45
B	THR65
B	GCP801

---

site_id	AC3
Number of Residues	3
Details	binding site for residue MG P 802

Chain	Residue
P	SER45
P	THR65
P	GCP801

---

site_id	AC4
Number of Residues	22
Details	binding site for Di-peptide GCP P 801 and LYS P 44

Chain	Residue
B	ASP211
P	VAL37
P	GLY39
P	SER41
P	GLY43
P	SER45
P	SER46
P	VAL47
P	LEU48
P	ARG59
P	GLY60
P	VAL64
P	THR65
P	LEU137
P	GLY139
P	LYS206
P	ASP208
P	ASN236
P	ARG237
P	SER238
P	GLN239
P	MG802

---

Functional Information from PROSITE/UniProt

site_id	PS00410
Number of Residues	10
Details	G_DYNAMIN_1 Dynamin-type guanine nucleotide-binding (G) domain signature. LPRGSGIVTR

Chain	Residue	Details
B	LEU57-ARG66

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0007744|PDB:5D3Q

Chain	Residue	Details
B	SER41
P	SER41

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:2X2F, ECO:0007744|PDB:5D3Q

Chain	Residue	Details
B	GLY43
B	SER45
B	LYS206
B	ASP208
P	GLY43
P	SER45
P	LYS206
P	ASP208

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0000269|PubMed:30069048, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:2X2F, ECO:0007744|PDB:5D3Q, ECO:0007744|PDB:6DLU

Chain	Residue	Details
B	LYS44
P	GLN239
B	SER46
B	ASN236
B	ARG237
B	GLN239
P	LYS44
P	SER46
P	ASN236
P	ARG237

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:26612256, ECO:0007744|PDB:5D3Q

Chain	Residue	Details
B	ARG59
P	ARG59

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:2X2F

Chain	Residue	Details
B	GLY60
P	GLY60

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0000269|PubMed:30069048, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:5D3Q, ECO:0007744|PDB:6DLU

Chain	Residue	Details
B	ASP211
P	ASP211

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P39053

Chain	Residue	Details
B	TYR80
B	TYR354
P	TYR80
P	TYR354

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; alternate => ECO:0000250|UniProtKB:P39053

Chain	Residue	Details
B	TYR125
P	TYR125

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P39053

Chain	Residue	Details
B	SER306
B	SER512
P	SER306
P	SER512

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21575

Chain	Residue	Details
B	SER347
P	SER347

---