5ORF

Structure of ovine serum albumin in P1 space group

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0008289	molecular_function	lipid binding
A	0046872	molecular_function	metal ion binding
A	0072562	cellular_component	blood microparticle
A	1903981	molecular_function	enterobactin binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0008289	molecular_function	lipid binding
B	0046872	molecular_function	metal ion binding
B	0072562	cellular_component	blood microparticle
B	1903981	molecular_function	enterobactin binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0008289	molecular_function	lipid binding
C	0046872	molecular_function	metal ion binding
C	0072562	cellular_component	blood microparticle
C	1903981	molecular_function	enterobactin binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005737	cellular_component	cytoplasm
D	0008289	molecular_function	lipid binding
D	0046872	molecular_function	metal ion binding
D	0072562	cellular_component	blood microparticle
D	1903981	molecular_function	enterobactin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue PGE A 601

Chain	Residue
A	ASN390
A	PHE402
A	ARG409
A	TYR410
A	LYS413
A	SER488

---

site_id	AC2
Number of Residues	4
Details	binding site for residue PGE A 602

Chain	Residue
A	HOH756
A	CYS264
A	ASP265
A	GLN267

---

site_id	AC3
Number of Residues	3
Details	binding site for residue PEG A 603

Chain	Residue
A	ASN158
A	ASN161
A	GLU284

---

site_id	AC4
Number of Residues	3
Details	binding site for residue PRO A 604

Chain	Residue
A	ALA576
A	GLN579
A	ALA580

---

site_id	AC5
Number of Residues	2
Details	binding site for residue PRO A 605

Chain	Residue
A	HIS3
C	ASP502

---

site_id	AC6
Number of Residues	4
Details	binding site for residue PRO A 606

Chain	Residue
A	PRO303
A	ALA306
A	HOH728
A	HOH747

---

site_id	AC7
Number of Residues	4
Details	binding site for residue PGE B 601

Chain	Residue
B	PHE402
B	ARG409
B	TYR410
B	SER488

---

site_id	AC8
Number of Residues	4
Details	binding site for residue PRO B 602

Chain	Residue
B	PHE501
B	ASP502
B	HOH716
D	HIS3

---

site_id	AC9
Number of Residues	4
Details	binding site for residue PRO B 604

Chain	Residue
B	ASN300
B	LEU301
B	PRO302
B	PRO303

---

site_id	AD1
Number of Residues	4
Details	binding site for residue PGE C 601

Chain	Residue
C	ASN390
C	ARG409
C	TYR410
C	SER488

---

site_id	AD2
Number of Residues	6
Details	binding site for residue PGE C 602

Chain	Residue
C	ALA405
C	VAL408
C	ARG409
C	ASP540
C	LEU543
C	MET547

---

site_id	AD3
Number of Residues	2
Details	binding site for residue PEG C 603

Chain	Residue
C	PRO303
C	ALA306

---

site_id	AD4
Number of Residues	4
Details	binding site for residue PRO C 604

Chain	Residue
C	ASN18
C	ASN158
C	VAL282
C	LEU283

---

site_id	AD5
Number of Residues	7
Details	binding site for residue PRO C 605

Chain	Residue
C	GLU118
C	PRO119
C	ASP120
C	GLU171
C	ASP172
C	LYS173
C	GLY174

---

site_id	AD6
Number of Residues	2
Details	binding site for residue PRO C 606

Chain	Residue
C	GLU564
C	VAL568

---

site_id	AD7
Number of Residues	7
Details	binding site for residue PGE D 601

Chain	Residue
D	LEU386
D	ASN390
D	ARG409
D	TYR410
D	LEU429
D	LEU452
D	SER488

---

site_id	AD8
Number of Residues	3
Details	binding site for residue PRO D 602

Chain	Residue
D	ASN300
D	LEU301
D	PRO302

---

site_id	AD9
Number of Residues	5
Details	binding site for residue PRO D 603

Chain	Residue
D	ALA405
D	VAL408
D	ARG409
D	ARG412
D	ASP540

---

Functional Information from PROSITE/UniProt

site_id	PS00212
Number of Residues	25
Details	ALBUMIN_1 Albumin domain signature. YngvfqeCCqaEdkgaCLlpkidaM

Chain	Residue	Details
A	TYR160-MET184
A	TYR352-LEU376
A	PHE550-LEU574

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P02770

Chain	Residue	Details
A	HIS3
B	HIS3
C	HIS3
D	HIS3

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P02769

Chain	Residue	Details
C	GLU6
C	ASP13
C	GLU243
C	GLU251
C	ASP254
C	ASP258
D	GLU6
D	ASP13
D	GLU243
D	GLU251
D	ASP254
D	ASP258
A	GLU243
A	GLU251
A	GLU6
A	ASP13
A	ASP254
A	ASP258
B	GLU6
B	ASP13
B	GLU243
B	GLU251
B	ASP254
B	ASP258

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P02768

Chain	Residue	Details
A	HIS246
A	ASP248
B	HIS67
A	HIS67
B	HIS246
B	ASP248
C	HIS67
C	HIS246
C	ASP248
D	HIS67
D	HIS246
D	ASP248

---

site_id	SWS_FT_FI4
Number of Residues	20
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02768

Chain	Residue	Details
A	SER488
B	SER5
B	SER58
B	SER65
B	SER418
B	SER488
C	SER5
C	SER58
C	SER65
C	SER418
C	SER488
D	SER5
D	SER58
D	SER65
D	SER418
D	SER488
A	SER5
A	SER58
A	SER65
A	SER418

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P02768

Chain	Residue	Details
B	THR419
B	THR421
C	THR83
C	THR419
C	THR421
D	THR83
D	THR419
D	THR421
A	THR83
A	THR419
A	THR421
B	THR83

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724

Chain	Residue	Details
B	LYS435
B	LYS563
C	LYS204
C	LYS435
C	LYS563
D	LYS204
D	LYS435
D	LYS563
A	LYS204
A	LYS435
A	LYS563
B	LYS204

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724

Chain	Residue	Details
A	SER272
B	SER272
C	SER272
D	SER272

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P02768

Chain	Residue	Details
A	LYS533
B	LYS533
C	LYS533
D	LYS533

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P02770

Chain	Residue	Details
A	THR545
B	THR545
C	THR545
D	THR545

---