2AFH
Crystal Structure of Nucleotide-Free Av2-Av1 Complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051536 | molecular_function | iron-sulfur cluster 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 | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster 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 | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051536 | molecular_function | iron-sulfur cluster 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 | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0051536 | molecular_function | iron-sulfur cluster 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 | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
E | 0046872 | molecular_function | metal ion binding |
E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster 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 | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
F | 0046872 | molecular_function | metal ion 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. SECpigliGDDIeSV |
Chain | Residue | Details |
A | SER152-VAL166 | |
B | THR151-PHE165 |
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. ISHGPVGC |
Chain | Residue | Details |
A | ILE81-CYS88 | |
B | TYR88-CYS95 |
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 | 6 |
Details | BINDING: |
Chain | Residue | Details |
E | LYS10 | |
C | SER443 | |
E | ALA98 | |
E | GLY133 | |
F | LYS10 | |
F | ALA98 | |
F | GLY133 | |
D | MET154 | |
D | PHE189 | |
C | TYR276 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250 |
Chain | Residue | Details |
E | GLY101 | |
F | GLY101 |
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 | GLY11 | electrostatic stabiliser, hydrogen bond donor |
E | SER16 | electrostatic stabiliser, hydrogen bond donor |
E | ALA42 | electrostatic stabiliser, hydrogen bond donor |
E | VAL130 | 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 | GLY11 | electrostatic stabiliser, hydrogen bond donor |
F | SER16 | electrostatic stabiliser, hydrogen bond donor |
F | ALA42 | electrostatic stabiliser, hydrogen bond donor |
F | VAL130 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |