4C3Z

Nucleotide-free crystal structure of nucleotide-binding domain 1 from human MRP1 supports a general-base catalysis mechanism for ATP hydrolysis.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1872

Chain	Residue
A	GLN679
A	VAL680
A	HIS827
A	TYR869

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1873

Chain	Residue
A	SER769
A	ARG775
A	VAL798
A	ASP799

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 1874

Chain	Residue
A	LYS820
A	HOH2057
A	ASN819

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 1875

Chain	Residue
A	GLY681
A	CYS682
A	GLY683
A	LYS684
A	SER685
A	SER686
A	HOH2018
A	HOH2020

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 1876

Chain	Residue
A	LYS697
A	HIS701
A	VAL702

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1877

Chain	Residue
A	PRO754
A	SER755
A	THR759
A	GLU760

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	26
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGCGKSSLLSaLlaemdkvegh........VAIK

Chain	Residue	Details
A	VAL680-LYS705

---

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRVSLARAV

Chain	Residue	Details
A	LEU768-VAL782

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	224
Details	Domain: {"description":"ABC transporter 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {}

Chain

Residue

Details

---