1F9B

MELANIN PROTEIN INTERACTION: X-RAY STRUCTURE OF THE COMPLEX OF MARE LACTOFERRIN WITH MELANIN MONOMERS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 690

Chain	Residue
A	ASP60
A	TYR92
A	TYR192
A	HIS253
A	BCT692

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 691

Chain	Residue
A	BCT693
A	ASP395
A	TYR433
A	TYR526
A	HIS595

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT A 692

Chain	Residue
A	ASP60
A	TYR92
A	THR117
A	ARG121
A	ALA123
A	GLY124
A	TYR192
A	HIS253
A	FE690

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT A 693

Chain	Residue
A	ASP395
A	TYR433
A	THR459
A	ARG463
A	THR464
A	ALA465
A	ALA466
A	TYR526
A	FE691

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 3ID A 694

Chain	Residue
A	TRP8
A	CYS9
A	THR10
A	ILE11
A	GLU15
A	VAL57
A	THR58
A	LEU299
A	PHE300

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 3ID A 695

Chain	Residue
A	VAL350
A	GLU354
A	ARG463
A	SER519
A	TYR524
A	GLY525
A	LYS637
A	ASN638
A	HOH696
A	HOH709
A	HOH730
A	HOH740

---

Functional Information from PROSITE/UniProt

site_id	PS00207
Number of Residues	31
Details	TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. KYeLLCpDntrkp...VdafkeChlArvpsHaVV

Chain	Residue	Details
A	LYS226-VAL256
A	ASP568-VAL598

---

site_id	PS00205
Number of Residues	10
Details	TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG

Chain	Residue	Details
A	TYR92-GLY101
A	TYR433-SER442

---

site_id	PS00206
Number of Residues	17
Details	TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLengaGDVAF

Chain	Residue	Details
A	TYR192-PHE208
A	TYR526-PHE542

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00741

Chain	Residue	Details
A	LYS73

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00741

Chain	Residue	Details
A	SER259

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531474, ECO:0000269|PubMed:11599026, ECO:0000269|Ref.7

Chain	Residue	Details
A	ASP60
A	TYR92
A	TYR192
A	HIS253
A	ASP395
A	TYR433
A	TYR526
A	HIS595

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10366507, ECO:0000269|PubMed:10531475

Chain	Residue	Details
A	THR117
A	ARG121
A	ALA123
A	GLY124
A	THR459
A	ARG463
A	ALA465
A	ALA466

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|Ref.7

Chain	Residue	Details
A	PRO430
A	ASN594
A	TYR660

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN137
A	ASN281
A	ASN476

---