Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2AFH

Crystal Structure of Nucleotide-Free Av2-Av1 Complex

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
E	0000166	molecular_function	nucleotide binding
E	0005524	molecular_function	ATP binding
E	0009399	biological_process	nitrogen fixation
E	0016163	molecular_function	nitrogenase activity
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	0000166	molecular_function	nucleotide binding
F	0005524	molecular_function	ATP binding
F	0009399	biological_process	nitrogen fixation
F	0016163	molecular_function	nitrogenase activity
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 2490

Chain	Residue
B	ARG108
B	GLU109
B	HOH5021
D	ASP353
D	ASP357
D	HOH5022

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 2491

Chain	Residue
D	ARG108
D	GLU109
D	HOH5023
B	ASP353
B	ASP357
B	HOH5022

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA B 2492

Chain	Residue
A	HOH5370
B	HOH5612
B	HOH5613
B	HOH5614

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HCA A 2494

Chain	Residue
A	ALA65
A	GLN191
A	GLY424
A	ILE425
A	HIS442
A	CFN2496
A	HOH5038
A	HOH5049
A	HOH5071
A	HOH5084
A	HOH5094
A	HOH5264
A	HOH5267
B	HOH5431
B	HOH5465
B	HOH5482

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CFN A 2496

Chain	Residue
A	VAL70
A	ARG96
A	HIS195
A	TYR229
A	CYS275
A	SER278
A	GLY356
A	GLY357
A	LEU358
A	ARG359
A	PHE381
A	HIS442
A	HCA2494

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLF B 2498

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	16
Details	BINDING SITE FOR RESIDUE HCA C 3494

Chain	Residue
C	ALA65
C	GLN191
C	GLY424
C	ILE425
C	HIS442
C	CFN3496
C	HOH5030
C	HOH5045
C	HOH5059
C	HOH5063
C	HOH5064
C	HOH5067
C	HOH5203
C	HOH5209
C	HOH5278
D	HOH5138

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CFN C 3496

Chain	Residue
C	VAL70
C	ARG96
C	HIS195
C	TYR229
C	CYS275
C	GLY356
C	GLY357
C	LEU358
C	ARG359
C	PHE381
C	HIS442
C	HCA3494

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLF C 3498

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

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 E 3290

Chain	Residue
E	CYS97
E	ALA98
E	CYS132
E	GLY134
F	CYS97
F	ALA98
F	CYS132
F	GLY134

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS B 5003

Chain	Residue
B	MET213
B	LYS216
B	VAL218
B	LYS310
B	HOH5063
B	HOH5155
B	HOH5425
B	HOH5495
B	HOH5590

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE TRS C 5004

Chain	Residue
C	GLU287
C	PRO293
C	TRP294

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE B 5005

Chain	Residue
B	PRO295
B	TRP296
B	GLU299
B	LYS315
B	ASN317
B	HOH5225

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE D 5006

Chain	Residue
D	PRO295
D	TRP296
D	LYS315
D	LEU316
D	HOH5383
D	HOH5478

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 E 5007

Chain	Residue
E	MET29
E	GLY30
E	LYS31
E	ASP120
E	VAL248
E	HOH5101

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGE D 5008

Chain	Residue
D	GLU33
D	LYS34
D	TYR35
D	HOH5535

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE P6G D 5009

Chain	Residue
D	GLN53
D	GLY307
D	LYS310
D	HIS311
D	GLU312
D	VAL421
D	TYR422
D	ILE423
D	HOH5223
D	HOH5316

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PGE D 5010

Chain	Residue
D	PHE183
D	TYR207

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE C 5011

Chain	Residue
C	LEU467
C	ASN468
C	TRP472
C	LYS473
C	HOH5340

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGE A 5012

Chain	Residue
A	ASP204
A	TRP205
A	HOH5161

site_id	CC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1PE C 5013

Chain	Residue
B	HIS363
B	GLU389
B	PRO414
B	TYR415
B	LYS417
C	ARG345
C	ASP464
C	ASN468
C	HOH5305
C	HOH5310
C	HOH5344

site_id	CC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PG4 B 5014

Chain	Residue
B	GLU299
B	LYS300
B	LYS303
B	ARG401
B	HOH5282
B	HOH5394
F	GLU110
F	TYR115
F	HOH352

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE A 5015

Chain	Residue
A	THR303
A	ILE306
A	GLU307
A	TRP335
A	HOH5155
A	HOH5340

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE C 5016

Chain	Residue
C	THR303
C	ILE306
C	TRP335
C	ASP369
C	HOH5090
C	HOH5121

site_id	CC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 1PE B 5017

Chain	Residue
B	THR48
B	THR49
B	PHE435
B	THR436
B	ASP437
B	LYS438
B	LYS458
B	GLU461
B	PHE462
B	HOH5061
B	HOH5080
B	HOH5124
B	HOH5177
E	GLU287
E	GLU288
E	HOH5121

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 5018

Chain	Residue
B	PHE57
B	TYR422
B	HOH5289

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG D 5019

Chain	Residue
D	GLU42
D	TRP46
D	LYS222

site_id	DC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG D 5020

Chain	Residue
A	PRO470
D	LYS381
D	LEU384
D	GLU385
D	SER413
D	HOH5183
D	HOH5200

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	PS00692
Number of Residues	14
Details	NIFH_FRXC_2 NifH/frxC family signature 2. DvLGDVVCGGFAmP

Chain	Residue	Details
E	ASP125-PRO138

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

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

Chain	Residue	Details
E	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	2
Details	Modified residue: {"description":"ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
E	LYS15
E	GLY12

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
F	LYS15
F	GLY12

site_id	MCSA1
Number of Residues	4
Details	M-CSA 212

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

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