5K65

Crystal structure of VEGF binding IgG1-Fc (Fcab CT6)

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, B	Ig gamma-1 chain C region	polymer	228	26008.6	2	UniProt (P01857) Pfam (PF07654) In PDB	Homo sapiens (Human)
2	C	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose	branched		1260.2	1	In PDB GlyTouCan (G45889JQ)
3	D	alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose	branched		910.8	1	In PDB GlyTouCan (G22768VO)
4		water	water		18.0	81	Chemie (HOH)

Sequence modifications

A, B: 225 - 447 (UniProt: P01857)

PDB	External Database	Details
Arg 359	Thr 242	engineered mutation
Phe 360	Lys 243	engineered mutation
Tyr 361	Asn 244	engineered mutation
Asp 388	Glu 271	engineered mutation
Ile 389	Asn 272	engineered mutation
Phe 389	-	insertion
Pro 389	-	insertion
Asn 389	-	insertion
Gly 389	-	insertion
Leu 389	-	insertion
Pro 413	Asp 296	engineered mutation
Tyr 414	Lys 297	engineered mutation
Pro 415	Ser 298	engineered mutation
Ser 416	Arg 299	engineered mutation
Leu 418	Gln 301	engineered mutation
Met 419	Gln 302	engineered mutation
Thr 421	Asn 304	engineered mutation
Arg 422	Val 305	engineered mutation
His 440	Ser 323	engineered mutation
Glu 442	Ser 325	engineered mutation
Tyr 443	Leu 326	engineered mutation
Gln 444	Ser 327	engineered mutation
Trp 445	Pro 328	engineered mutation
Pro 446	Gly 329	engineered mutation
Thr 447	Lys 330	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	52017.2
Branched	Number of molecules	2
	Total formula weight	2171.0
All*	Total formula weight	54188.1

*Water molecules are not included.