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 | 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 | 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 | 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 | 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 | 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 | 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. 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 |
| A | ILE81-CYS88 | |
| B | TYR88-CYS95 |
| 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 | 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 |
| D | MET154 | |
| D | PHE189 | |
| C | TYR276 | |
| C | SER443 | |
| E | LYS10 | |
| E | ALA98 | |
| E | GLY133 | |
| F | LYS10 | |
| F | ALA98 | |
| F | GLY133 |
| 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 | 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 |
