5AUP

Crystal structure of the HypAB complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0016151	molecular_function	nickel cation binding
A	0036211	biological_process	protein modification process
A	0046872	molecular_function	metal ion binding
A	0051604	biological_process	protein maturation
B	0005524	molecular_function	ATP binding
B	0016226	biological_process	iron-sulfur cluster assembly
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0140663	molecular_function	ATP-dependent FeS chaperone activity
H	0008270	molecular_function	zinc ion binding
H	0016151	molecular_function	nickel cation binding
H	0036211	biological_process	protein modification process
H	0046872	molecular_function	metal ion binding
H	0051604	biological_process	protein maturation
I	0005524	molecular_function	ATP binding
I	0016226	biological_process	iron-sulfur cluster assembly
I	0016787	molecular_function	hydrolase activity
I	0016887	molecular_function	ATP hydrolysis activity
I	0046872	molecular_function	metal ion binding
I	0051536	molecular_function	iron-sulfur cluster binding
I	0051539	molecular_function	4 iron, 4 sulfur cluster binding
I	0140663	molecular_function	ATP-dependent FeS chaperone activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 201

Chain	Residue
A	CYS73
A	CYS76
A	CYS110
A	CYS113

---

site_id	AC2
Number of Residues	23
Details	binding site for residue ACP B 301

Chain	Residue
B	LEU35
B	ASP57
B	PRO135
B	ASN187
B	MET188
B	PRO217
B	TYR219
B	LEU222
B	ASP223
B	PHE237
B	MG302
B	HOH401
B	HOH402
B	HOH403
I	LYS28
I	GLY29
I	SER160
I	LEU162
B	GLY30
B	VAL31
B	GLY32
B	LYS33
B	SER34

---

site_id	AC3
Number of Residues	5
Details	binding site for residue MG B 302

Chain	Residue
B	SER34
B	ACP301
B	HOH401
B	HOH402
B	HOH403

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN H 201

Chain	Residue
H	CYS73
H	CYS76
H	CYS110
H	CYS113

---

site_id	AC5
Number of Residues	20
Details	binding site for residue ACP I 301

Chain	Residue
B	LYS28
B	GLY29
B	SER160
I	GLY29
I	GLY30
I	GLY32
I	LYS33
I	SER34
I	LEU35
I	ASP57
I	PRO135
I	ASN187
I	MET188
I	PRO217
I	TYR219
I	ASP223
I	MG302
I	HOH401
I	HOH402
I	HOH403

---

site_id	AC6
Number of Residues	6
Details	binding site for residue MG I 302

Chain	Residue
I	SER34
I	ASP57
I	ACP301
I	HOH401
I	HOH402
I	HOH403

---

Functional Information from PROSITE/UniProt

site_id	PS01249
Number of Residues	43
Details	HYPA Hydrogenases expression/synthesis hypA family signature. GelqdVaediVkfAMeqlfagTiaeg.AeIeFveeeavfkCrnC

Chain	Residue	Details
A	GLY34-CYS76

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:26056269, ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO

Chain	Residue	Details
A	MET1
A	HIS2
A	HIS98
H	MET1
H	HIS2
H	HIS98

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00213, ECO:0000269|PubMed:19769985, ECO:0000269|PubMed:26056269, ECO:0007744|PDB:3A43, ECO:0007744|PDB:3A44, ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO, ECO:0007744|PDB:5AUP

Chain	Residue	Details
A	CYS73
A	CYS76
A	CYS110
A	CYS113
H	CYS73
H	CYS76
H	CYS110
H	CYS113

---