Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3U7Q

A. vinelandii nitrogenase MoFe protein at atomic resolution

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	0016612	cellular_component	molybdenum-iron nitrogenase complex
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-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	0016612	cellular_component	molybdenum-iron nitrogenase complex
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-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	0016612	cellular_component	molybdenum-iron nitrogenase complex
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-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	0016612	cellular_component	molybdenum-iron nitrogenase complex
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HCA A 6494

Chain	Residue
A	ALA65
A	HOH538
A	HOH561
A	HOH573
A	HOH585
A	ICS6496
B	HOH592
B	HOH674
A	GLN191
A	GLY424
A	ILE425
A	HIS442
A	HOH519
A	HOH525
A	HOH534
A	HOH536

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ICS A 6496

Chain	Residue
A	VAL70
A	ARG96
A	HIS195
A	TYR229
A	CYS275
A	GLY356
A	GLY357
A	ARG359
A	PHE381
A	HIS442
A	HCA6494

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IMD A 493

Chain	Residue
A	TRP294
A	HOH495
A	HOH2352

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IMD A 494

Chain	Residue
A	ARG96
A	TYR99
A	THR111
D	HOH552
D	HOH698
D	HOH878

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA B 7492

Chain	Residue
B	ASP353
B	ASP357
B	HOH608
D	ARG108
D	GLU109
D	HOH628
D	HOH1263

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 1CL B 6498

Chain	Residue
A	CYS62
A	TYR64
A	PRO85
A	GLY87
A	CYS88
A	TYR91
A	CYS154
A	GLY185
B	CYS70
B	SER92
B	CYS95
B	TYR98
B	CYS153
B	SER188

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLF B 6499

Chain	Residue
A	CYS62
A	TYR64
A	PRO85
A	GLY87
A	CYS88
A	TYR91
A	CYS154
A	GLY185
B	CYS70
B	SER92
B	CYS95
B	TYR98
B	CYS153
B	SER188

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA B 6492

Chain	Residue
B	ARG108
B	GLU109
B	HOH627
D	ASP353
D	ASP357
D	HOH711
D	HOH2575

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IMD B 524

Chain	Residue
B	SER482
B	THR483
B	GLN492
B	THR496
B	HOH530

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IMD B 525

Chain	Residue
A	GLY157
B	GLU120
B	ALA123
C	GLN41
C	LYS44

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 526

Chain	Residue
B	HOH659
B	HOH837

site_id	BC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HCA C 7494

Chain	Residue
C	HOH537
C	HOH546
C	HOH558
C	HOH570
C	ICS7496
D	HOH574
D	HOH634
C	ALA65
C	GLN191
C	GLY424
C	ILE425
C	HIS442
C	HOH497
C	HOH505
C	HOH517
C	HOH535

site_id	BC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ICS C 7496

Chain	Residue
C	VAL70
C	ARG96
C	HIS195
C	TYR229
C	CYS275
C	GLY356
C	GLY357
C	ARG359
C	PHE381
C	HIS442
C	HCA7494

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IMD C 493

Chain	Residue
C	TRP294
C	HOH607
C	HOH1611

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IMD C 494

Chain	Residue
A	GLN41
A	LYS44
C	GLY157
D	GLU120
D	ALA123

site_id	BC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 1CL D 7498

Chain	Residue
C	CYS62
C	TYR64
C	PRO85
C	GLY87
C	CYS88
C	TYR91
C	CYS154
C	GLY185
D	CYS70
D	SER92
D	CYS95
D	TYR98
D	CYS153
D	SER188

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IMD D 524

Chain	Residue
D	SER482
D	THR483
D	GLN492
D	THR496
D	HOH527

site_id	BC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLF D 7499

Chain	Residue
C	CYS62
C	TYR64
C	PRO85
C	GLY87
C	CYS88
C	TYR91
C	CYS154
C	GLY185
D	CYS70
D	SER92
D	CYS95
D	TYR98
D	CYS153
D	SER188

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IMD D 525

Chain	Residue
D	LEU253
D	ASP256
D	GLY275
D	THR276
D	GLU280

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 526

Chain	Residue
D	LYS9
D	HOH707

Functional Information from PROSITE/UniProt

site_id	PS00090
Number of Residues	15
Details	NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. TTCmaeviGDDLnAF

Chain	Residue	Details
B	THR151-PHE165
A	SER152-VAL166

site_id	PS00699
Number of Residues	8
Details	NITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. YVHGSQGC

Chain	Residue	Details
B	TYR88-CYS95
A	ILE81-CYS88

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 212

Chain	Residue	Details
B	CYS153	metal ligand
B	VAL157	polar interaction, single electron acceptor, single electron donor, single electron relay
A	ARG96	activator, hydrogen bond donor
A	HIS195	activator, polar interaction

site_id	MCSA2
Number of Residues	2
Details	M-CSA 212

Chain	Residue	Details
D	CYS153	metal ligand
D	VAL157	polar interaction, single electron acceptor, single electron donor, single electron relay
C	ARG96	activator, hydrogen bond donor
C	HIS195	activator, polar interaction

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)