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 | 0000166 | molecular_function | nucleotide binding |
| 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_FI6 |
| Number of Residues | 25 |
| Details | Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
