4H0X
Crystal structure of NAD+-Ia(E380A)-actin complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005576 | cellular_component | extracellular region |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0001725 | cellular_component | stress fiber |
B | 0003785 | molecular_function | actin monomer binding |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005523 | molecular_function | tropomyosin binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005856 | cellular_component | cytoskeleton |
B | 0005865 | cellular_component | striated muscle thin filament |
B | 0005884 | cellular_component | actin filament |
B | 0010628 | biological_process | positive regulation of gene expression |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019904 | molecular_function | protein domain specific binding |
B | 0030027 | cellular_component | lamellipodium |
B | 0030041 | biological_process | actin filament polymerization |
B | 0030175 | cellular_component | filopodium |
B | 0030240 | biological_process | skeletal muscle thin filament assembly |
B | 0031013 | molecular_function | troponin I binding |
B | 0031432 | molecular_function | titin binding |
B | 0031941 | cellular_component | filamentous actin |
B | 0032036 | molecular_function | myosin heavy chain binding |
B | 0032432 | cellular_component | actin filament bundle |
B | 0042802 | molecular_function | identical protein binding |
B | 0044297 | cellular_component | cell body |
B | 0048306 | molecular_function | calcium-dependent protein binding |
B | 0048741 | biological_process | skeletal muscle fiber development |
B | 0051017 | biological_process | actin filament bundle assembly |
B | 0090131 | biological_process | mesenchyme migration |
B | 0098723 | cellular_component | skeletal muscle myofibril |
B | 0140660 | molecular_function | cytoskeletal motor activator activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NAD A 501 |
Chain | Residue |
A | TYR251 |
A | THR339 |
A | PHE349 |
A | ARG352 |
A | EDO503 |
A | ILE259 |
A | ARG295 |
A | ARG296 |
A | GLY298 |
A | GLN300 |
A | GLU301 |
A | ASN335 |
A | SER338 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 502 |
Chain | Residue |
A | ARG5 |
A | TRP19 |
A | GLU23 |
A | ILE85 |
A | ASP86 |
A | HOH680 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | TYR294 |
A | ARG296 |
A | SER340 |
A | GLY342 |
A | SER343 |
A | VAL344 |
A | PHE349 |
A | NAD501 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
Chain | Residue |
A | MET346 |
A | SER347 |
A | ALA348 |
B | MET176 |
B | ARG177 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | TYR60 |
A | ASP61 |
A | MET346 |
A | SER347 |
A | HOH697 |
B | MET176 |
B | LYS284 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | ILE80 |
A | THR164 |
A | GLY165 |
A | GLU180 |
A | ASP182 |
A | HOH608 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | TYR42 |
A | SER46 |
A | TYR169 |
A | ASN171 |
A | LYS176 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 508 |
Chain | Residue |
A | TYR60 |
A | GLN63 |
A | ASN345 |
A | ALA350 |
A | LYS351 |
A | ASP399 |
A | HOH626 |
A | HOH634 |
B | GLU276 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 509 |
Chain | Residue |
A | ASN90 |
A | HIS157 |
A | GLU204 |
A | ALA205 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 510 |
Chain | Residue |
A | LYS159 |
A | SER206 |
A | ILE207 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 511 |
Chain | Residue |
A | LYS132 |
A | ASP182 |
A | TYR183 |
A | SER184 |
A | SER210 |
A | HOH609 |
A | HOH673 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 401 |
Chain | Residue |
B | ATP402 |
B | HOH521 |
B | HOH522 |
B | HOH524 |
B | HOH525 |
B | HOH526 |
site_id | BC4 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE ATP B 402 |
Chain | Residue |
B | EDO414 |
B | HOH518 |
B | HOH521 |
B | HOH522 |
B | HOH526 |
B | HOH527 |
B | HOH558 |
B | HOH559 |
B | GLY13 |
B | SER14 |
B | GLY15 |
B | LEU16 |
B | LYS18 |
B | GLY156 |
B | ASP157 |
B | GLY158 |
B | VAL159 |
B | GLY182 |
B | ARG210 |
B | LYS213 |
B | GLU214 |
B | GLY301 |
B | GLY302 |
B | THR303 |
B | MET305 |
B | TYR306 |
B | LYS336 |
B | CA401 |
site_id | BC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE LAR B 403 |
Chain | Residue |
B | GLY15 |
B | LEU16 |
B | PRO32 |
B | ASP56 |
B | GLN59 |
B | ARG62 |
B | LEU67 |
B | TYR69 |
B | ASP157 |
B | ARG183 |
B | THR186 |
B | ARG206 |
B | GLU207 |
B | ARG210 |
B | HOH555 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 404 |
Chain | Residue |
B | HIS73 |
B | GLY158 |
B | ASP184 |
B | HOH581 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 405 |
Chain | Residue |
B | ARG183 |
B | ARG206 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 406 |
Chain | Residue |
B | SER141 |
B | LEU142 |
B | SER145 |
B | VAL298 |
B | MET299 |
B | SER300 |
B | PRO332 |
B | SER338 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 407 |
Chain | Residue |
B | MET283 |
B | ARG290 |
B | TYR294 |
B | PRO322 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 408 |
Chain | Residue |
B | THR318 |
B | ALA321 |
B | PRO322 |
B | SER323 |
B | MET325 |
B | ILE327 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 409 |
Chain | Residue |
B | THR148 |
B | THR149 |
B | ASN296 |
B | HOH585 |
site_id | CC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 410 |
Chain | Residue |
B | ARG62 |
B | TYR166 |
B | THR203 |
B | ALA204 |
B | ASP288 |
B | ASP292 |
B | HOH539 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 411 |
Chain | Residue |
B | GLU83 |
B | HIS87 |
B | EDO412 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 412 |
Chain | Residue |
B | TYR91 |
B | GLU99 |
B | THR126 |
B | PHE127 |
B | SER350 |
B | EDO411 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 413 |
Chain | Residue |
B | TYR198 |
B | SER199 |
B | PHE200 |
site_id | CC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 414 |
Chain | Residue |
B | LYS213 |
B | GLU214 |
B | CYS217 |
B | MET305 |
B | TYR306 |
B | PRO307 |
B | ATP402 |
B | HOH516 |
site_id | CC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 415 |
Chain | Residue |
B | GLN263 |
B | PRO264 |
B | SER265 |
B | EDO416 |
B | HOH590 |
site_id | CC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 416 |
Chain | Residue |
A | LYS351 |
B | PHE262 |
B | ALA272 |
B | GLY273 |
B | HIS275 |
B | GLU276 |
B | EDO415 |
Functional Information from PROSITE/UniProt
site_id | PS00406 |
Number of Residues | 11 |
Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
Chain | Residue | Details |
B | TYR53-GLY63 |
site_id | PS00432 |
Number of Residues | 9 |
Details | ACTINS_2 Actins signature 2. WITKqEYDE |
Chain | Residue | Details |
B | TRP356-GLU364 |
site_id | PS01132 |
Number of Residues | 13 |
Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
Chain | Residue | Details |
B | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665 |
Chain | Residue | Details |
B | ASP1 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
Chain | Residue | Details |
B | MET44 | |
B | MET47 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
Chain | Residue | Details |
B | LYS61 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK |
Chain | Residue | Details |
B | HIS73 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
Chain | Residue | Details |
B | LYS84 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 |
Chain | Residue | Details |
B | ARG177 |