1XCP

Crystal Structure of the Nitrogenase Fe protein Phe135Trp with MgADP bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0009399	biological_process	nitrogen fixation
A	0016163	molecular_function	nitrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0009399	biological_process	nitrogen fixation
B	0016163	molecular_function	nitrogenase activity
B	0016491	molecular_function	oxidoreductase 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
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0009399	biological_process	nitrogen fixation
C	0016163	molecular_function	nitrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0009399	biological_process	nitrogen fixation
D	0016163	molecular_function	nitrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1293

Chain	Residue
A	LYS15
A	SER16
A	ASP39
A	ASP43
A	ADP1291

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 1294

Chain	Residue
B	ADP1292
B	LYS15
B	SER16
B	ASP39
B	ASP43

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 2293

Chain	Residue
C	SER16
C	ASP39
C	ASP43
C	ASP125
C	ADP2291

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 2294

Chain	Residue
D	SER16
D	ASP39
D	ASP43
D	ASP125
D	ADP2292

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 1290

Chain	Residue
A	CYS97
A	ALA98
A	CYS132
A	GLY134
B	CYS97
B	ALA98
B	CYS132
B	GLY134

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 C 2290

Chain	Residue
C	CYS97
C	ALA98
C	CYS132
C	GLY134
D	CYS97
D	ALA98
D	CYS132
D	GLY134

---

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP A 1291

Chain	Residue
A	LYS10
A	GLY12
A	ILE13
A	GLY14
A	LYS15
A	SER16
A	THR17
A	ASN185
A	VAL211
A	PRO212
A	ARG213
A	ASP214
A	VAL217
A	GLN218
A	GLU221
A	GLN236
A	TYR240
A	MG1293

---

site_id	AC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP B 1292

Chain	Residue
B	LYS10
B	GLY12
B	ILE13
B	GLY14
B	LYS15
B	SER16
B	THR17
B	ASN185
B	VAL211
B	PRO212
B	ARG213
B	ASP214
B	VAL217
B	GLN218
B	GLU221
B	GLN236
B	TYR240
B	MG1294

---

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP C 2291

Chain	Residue
C	LYS10
C	GLY12
C	ILE13
C	GLY14
C	LYS15
C	SER16
C	THR17
C	ASN185
C	PRO212
C	ARG213
C	ASP214
C	GLN218
C	GLU221
C	GLN236
C	TYR240
C	MG2293

---

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP D 2292

Chain	Residue
D	GLN218
D	GLU221
D	GLN236
D	TYR240
D	MG2294
D	LYS10
D	GLY12
D	ILE13
D	GLY14
D	LYS15
D	SER16
D	THR17
D	ASN185
D	PRO212
D	ARG213
D	ASP214

---

Functional Information from PROSITE/UniProt

site_id	PS00746
Number of Residues	13
Details	NIFH_FRXC_1 NifH/frxC family signature 1. EsGGPepGvGCAG

Chain	Residue	Details
A	GLU87-GLY99

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
A	LYS10	electrostatic stabiliser, hydrogen bond donor
A	LYS15	electrostatic stabiliser, hydrogen bond donor
A	LYS41	electrostatic stabiliser, hydrogen bond donor
A	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
B	LYS10	electrostatic stabiliser, hydrogen bond donor
B	LYS15	electrostatic stabiliser, hydrogen bond donor
B	LYS41	electrostatic stabiliser, hydrogen bond donor
B	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
C	LYS10	electrostatic stabiliser, hydrogen bond donor
C	LYS15	electrostatic stabiliser, hydrogen bond donor
C	LYS41	electrostatic stabiliser, hydrogen bond donor
C	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---

site_id	MCSA4
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
D	LYS10	electrostatic stabiliser, hydrogen bond donor
D	LYS15	electrostatic stabiliser, hydrogen bond donor
D	LYS41	electrostatic stabiliser, hydrogen bond donor
D	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---