3ZYC

DYNAMIN 1 GTPASE GED FUSION DIMER COMPLEXED WITH GMPPCP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003924	molecular_function	GTPase activity
A	0005525	molecular_function	GTP binding
D	0003924	molecular_function	GTPase activity
D	0005525	molecular_function	GTP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE GCP A 1749

Chain	Residue
A	GLN40
A	SER61
A	GLY62
A	VAL64
A	THR65
A	GLY139
A	LYS206
A	ASP208
A	LEU209
A	ASN236
A	ARG237
A	SER41
A	SER238
A	GLN239
A	ILE242
A	MG1750
A	HOH1751
A	HOH1752
A	HOH2036
A	HOH2227
D	ASP211
A	ALA42
A	GLY43
A	LYS44
A	SER45
A	SER46
A	ARG59
A	GLY60

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1750

Chain	Residue
A	SER45
A	THR65
A	GCP1749
A	HOH1751
A	HOH1752

---

site_id	AC3
Number of Residues	30
Details	BINDING SITE FOR RESIDUE GCP D 1749

Chain	Residue
A	ASP211
A	HOH2158
D	GLN40
D	SER41
D	ALA42
D	GLY43
D	LYS44
D	SER45
D	SER46
D	ARG59
D	GLY60
D	SER61
D	GLY62
D	VAL64
D	THR65
D	GLY139
D	LYS206
D	ASP208
D	LEU209
D	VAL235
D	ASN236
D	ARG237
D	SER238
D	GLN239
D	ILE242
D	MG1750
D	HOH1751
D	HOH1752
D	HOH2023
D	HOH2043

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1750

Chain	Residue
D	SER45
D	THR65
D	GCP1749
D	HOH1751
D	HOH1752

---

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
A	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
A	SER41
D	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
A	GLY43
A	SER45
A	LYS206
A	ASP208
D	GLY43
D	SER45
D	LYS206
D	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
A	LYS44
D	GLN239
A	SER46
A	ASN236
A	ARG237
A	GLN239
D	LYS44
D	SER46
D	ASN236
D	ARG237

---

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

Chain	Residue	Details
A	ARG59
D	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
A	GLY60
D	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
A	ASP211
D	ASP211

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P39053

Chain	Residue	Details
A	TYR80
D	TYR80

---

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

Chain	Residue	Details
A	TYR125
D	TYR125

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P39053

Chain	Residue	Details
A	SER306
D	SER306

---