5MM0

Dolichyl phosphate mannose synthase in complex with GDP-mannose and Mn2+ (donor complex)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000271	biological_process	polysaccharide biosynthetic process
A	0003824	molecular_function	catalytic activity
A	0004582	molecular_function	dolichyl-phosphate beta-D-mannosyltransferase activity
A	0005886	cellular_component	plasma membrane
A	0006486	biological_process	protein glycosylation
A	0006488	biological_process	dolichol-linked oligosaccharide biosynthetic process
A	0006506	biological_process	GPI anchor biosynthetic process
A	0016020	cellular_component	membrane
A	0016757	molecular_function	glycosyltransferase activity
A	0019348	biological_process	dolichol metabolic process
A	0035269	biological_process	protein O-linked mannosylation
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue GDD A 401

Chain	Residue
A	PRO8
A	ALA90
A	ASP91
A	GLN93
A	HIS94
A	ARG117
A	VAL156
A	GLY158
A	LYS178
A	ARG202
A	SER207
A	THR9
A	LYS208
A	MN402
A	TYR10
A	GLU12
A	VAL37
A	ASP39
A	LEU69
A	ALA72
A	ASP89

---

site_id	AC2
Number of Residues	4
Details	binding site for residue MN A 402

Chain	Residue
A	ASP91
A	GLN93
A	ARG202
A	GDD401

---

site_id	AC3
Number of Residues	3
Details	binding site for residue CL A 403

Chain	Residue
A	ASN277
A	PHE301
A	ARG341

---

site_id	AC4
Number of Residues	5
Details	binding site for residue LDA A 404

Chain	Residue
A	SER243
A	TRP280
A	TRP284
A	LDA407
A	LDA407

---

site_id	AC5
Number of Residues	6
Details	binding site for residue LDA A 405

Chain	Residue
A	LEU242
A	ILE245
A	GLU249
A	GLY250
A	PHE251
A	TRP253

---

site_id	AC6
Number of Residues	2
Details	binding site for residue LDA A 406

Chain	Residue
A	ARG150
A	HIS347

---

site_id	AC7
Number of Residues	4
Details	binding site for residue LDA A 407

Chain	Residue
A	PHE279
A	TRP284
A	LDA404
A	LDA404

---

site_id	AC8
Number of Residues	4
Details	binding site for residue LDA A 408

Chain	Residue
A	VAL270
A	SER273
A	LEU306
A	LEU306

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	235
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	MET1-GLY229
A	LYS287-SER293
A	ALA351-THR352

---

site_id	SWS_FT_FI2
Number of Residues	100
Details	TRANSMEM: Helical => ECO:0000305|PubMed:28743912

Chain	Residue	Details
A	GLU230-VAL256
A	LYS262-PHE286
A	ILE294-LEU320
A	TYR326-TRP350

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	TOPO_DOM: Extracellular => ECO:0000305

Chain	Residue	Details
A	ASN257-PRO261
A	PHE321-HIS325

---

site_id	SWS_FT_FI4
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:28743912, ECO:0007744|PDB:5MLZ, ECO:0007744|PDB:5MM0, ECO:0007744|PDB:5MM1

Chain	Residue	Details
A	PRO8
A	TYR10
A	VAL37
A	ASP39
A	ALA90

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:28743912, ECO:0007744|PDB:5MM0

Chain	Residue	Details
A	GLU12
A	ASP89
A	ASP91
A	GLN93

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:28743912, ECO:0007744|PDB:5MM0, ECO:0007744|PDB:5MM1

Chain	Residue	Details
A	ARG117
A	VAL156
A	LYS178

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:28743912, ECO:0007744|PDB:5MLZ, ECO:0007744|PDB:5MM0

Chain	Residue	Details
A	ARG202
A	LYS208

---