6G2H
Filament of acetyl-CoA carboxylase and BRCT domains of BRCA1 (ACC-BRCT) core at 4.6 A resolution
This is a non-PDB format compatible entry.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001650 | cellular_component | fibrillar center |
A | 0001894 | biological_process | tissue homeostasis |
A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005829 | cellular_component | cytosol |
A | 0006084 | biological_process | acetyl-CoA metabolic process |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0008610 | biological_process | lipid biosynthetic process |
A | 0015629 | cellular_component | actin cytoskeleton |
A | 0016874 | molecular_function | ligase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
A | 0051289 | biological_process | protein homotetramerization |
A | 0055088 | biological_process | lipid homeostasis |
A | 0071380 | biological_process | cellular response to prostaglandin E stimulus |
A | 2001295 | biological_process | malonyl-CoA biosynthetic process |
B | 0001650 | cellular_component | fibrillar center |
B | 0001894 | biological_process | tissue homeostasis |
B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005829 | cellular_component | cytosol |
B | 0006084 | biological_process | acetyl-CoA metabolic process |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0008610 | biological_process | lipid biosynthetic process |
B | 0015629 | cellular_component | actin cytoskeleton |
B | 0016874 | molecular_function | ligase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
B | 0051289 | biological_process | protein homotetramerization |
B | 0055088 | biological_process | lipid homeostasis |
B | 0071380 | biological_process | cellular response to prostaglandin E stimulus |
B | 2001295 | biological_process | malonyl-CoA biosynthetic process |
C | 0001650 | cellular_component | fibrillar center |
C | 0001894 | biological_process | tissue homeostasis |
C | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005829 | cellular_component | cytosol |
C | 0006084 | biological_process | acetyl-CoA metabolic process |
C | 0006629 | biological_process | lipid metabolic process |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0008610 | biological_process | lipid biosynthetic process |
C | 0015629 | cellular_component | actin cytoskeleton |
C | 0016874 | molecular_function | ligase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
C | 0051289 | biological_process | protein homotetramerization |
C | 0055088 | biological_process | lipid homeostasis |
C | 0071380 | biological_process | cellular response to prostaglandin E stimulus |
C | 2001295 | biological_process | malonyl-CoA biosynthetic process |
D | 0001650 | cellular_component | fibrillar center |
D | 0001894 | biological_process | tissue homeostasis |
D | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005829 | cellular_component | cytosol |
D | 0006084 | biological_process | acetyl-CoA metabolic process |
D | 0006629 | biological_process | lipid metabolic process |
D | 0006633 | biological_process | fatty acid biosynthetic process |
D | 0008610 | biological_process | lipid biosynthetic process |
D | 0015629 | cellular_component | actin cytoskeleton |
D | 0016874 | molecular_function | ligase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
D | 0051289 | biological_process | protein homotetramerization |
D | 0055088 | biological_process | lipid homeostasis |
D | 0071380 | biological_process | cellular response to prostaglandin E stimulus |
D | 2001295 | biological_process | malonyl-CoA biosynthetic process |
E | 0001650 | cellular_component | fibrillar center |
E | 0001894 | biological_process | tissue homeostasis |
E | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005739 | cellular_component | mitochondrion |
E | 0005829 | cellular_component | cytosol |
E | 0006084 | biological_process | acetyl-CoA metabolic process |
E | 0006629 | biological_process | lipid metabolic process |
E | 0006633 | biological_process | fatty acid biosynthetic process |
E | 0008610 | biological_process | lipid biosynthetic process |
E | 0015629 | cellular_component | actin cytoskeleton |
E | 0016874 | molecular_function | ligase activity |
E | 0042802 | molecular_function | identical protein binding |
E | 0046872 | molecular_function | metal ion binding |
E | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
E | 0051289 | biological_process | protein homotetramerization |
E | 0055088 | biological_process | lipid homeostasis |
E | 0071380 | biological_process | cellular response to prostaglandin E stimulus |
E | 2001295 | biological_process | malonyl-CoA biosynthetic process |
F | 0001650 | cellular_component | fibrillar center |
F | 0001894 | biological_process | tissue homeostasis |
F | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
F | 0005515 | molecular_function | protein binding |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005739 | cellular_component | mitochondrion |
F | 0005829 | cellular_component | cytosol |
F | 0006084 | biological_process | acetyl-CoA metabolic process |
F | 0006629 | biological_process | lipid metabolic process |
F | 0006633 | biological_process | fatty acid biosynthetic process |
F | 0008610 | biological_process | lipid biosynthetic process |
F | 0015629 | cellular_component | actin cytoskeleton |
F | 0016874 | molecular_function | ligase activity |
F | 0042802 | molecular_function | identical protein binding |
F | 0046872 | molecular_function | metal ion binding |
F | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
F | 0051289 | biological_process | protein homotetramerization |
F | 0055088 | biological_process | lipid homeostasis |
F | 0071380 | biological_process | cellular response to prostaglandin E stimulus |
F | 2001295 | biological_process | malonyl-CoA biosynthetic process |
Functional Information from PROSITE/UniProt
site_id | PS00188 |
Number of Residues | 18 |
Details | BIOTIN Biotin-requiring enzymes attachment site. GQcYaeIeVMKMvmtLtA |
Chain | Residue | Details |
D | GLY776-ALA793 |
site_id | PS00866 |
Number of Residues | 15 |
Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASeggGGkG |
Chain | Residue | Details |
D | TYR306-GLY320 |
site_id | PS00867 |
Number of Residues | 8 |
Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL |
Chain | Residue | Details |
D | PHE435-LEU442 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
D | ARG441 | |
E | ARG441 | |
C | ARG441 | |
F | ARG441 | |
B | ARG441 | |
A | ARG441 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 |
Chain | Residue | Details |
D | GLY315 | |
E | GLY315 | |
C | GLY315 | |
F | GLY315 | |
B | GLY315 | |
A | GLY315 |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969 |
Chain | Residue | Details |
D | GLU424 | |
F | GLU424 | |
F | GLU437 | |
F | ASN439 | |
B | GLU424 | |
B | GLU437 | |
B | ASN439 | |
A | GLU424 | |
A | GLU437 | |
A | ASN439 | |
D | GLU437 | |
D | ASN439 | |
E | GLU424 | |
E | GLU437 | |
E | ASN439 | |
C | GLU424 | |
C | GLU437 | |
C | ASN439 |
site_id | SWS_FT_FI4 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
D | ARG1823 | |
F | ARG1823 | |
F | LYS2127 | |
F | ARG2129 | |
B | ARG1823 | |
B | LYS2127 | |
B | ARG2129 | |
A | ARG1823 | |
A | LYS2127 | |
A | ARG2129 | |
D | LYS2127 | |
D | ARG2129 | |
E | ARG1823 | |
E | LYS2127 | |
E | ARG2129 | |
C | ARG1823 | |
C | LYS2127 | |
C | ARG2129 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: N-acetylmethionine => ECO:0000269|Ref.9, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
D | MET1 | |
E | MET1 | |
C | MET1 | |
F | MET1 | |
B | MET1 | |
A | MET1 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
D | SER5 | |
E | SER5 | |
C | SER5 | |
F | SER5 | |
B | SER5 | |
A | SER5 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
D | SER23 | |
E | SER23 | |
C | SER23 | |
F | SER23 | |
B | SER23 | |
A | SER23 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
D | SER25 | |
E | SER25 | |
C | SER25 | |
F | SER25 | |
B | SER25 | |
A | SER25 |
site_id | SWS_FT_FI9 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
D | SER29 | |
E | SER29 | |
C | SER29 | |
F | SER29 | |
B | SER29 | |
A | SER29 |
site_id | SWS_FT_FI10 |
Number of Residues | 30 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11497 |
Chain | Residue | Details |
D | SER34 | |
E | SER1216 | |
C | SER34 | |
C | SER50 | |
C | SER78 | |
C | SER1201 | |
C | SER1216 | |
F | SER34 | |
F | SER50 | |
F | SER78 | |
F | SER1201 | |
D | SER50 | |
F | SER1216 | |
B | SER34 | |
B | SER50 | |
B | SER78 | |
B | SER1201 | |
B | SER1216 | |
A | SER34 | |
A | SER50 | |
A | SER78 | |
A | SER1201 | |
D | SER78 | |
A | SER1216 | |
D | SER1201 | |
D | SER1216 | |
E | SER34 | |
E | SER50 | |
E | SER78 | |
E | SER1201 |
site_id | SWS_FT_FI11 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
D | SER48 | |
E | SER48 | |
C | SER48 | |
F | SER48 | |
B | SER48 | |
A | SER48 |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983 |
Chain | Residue | Details |
D | SER53 | |
E | SER53 | |
C | SER53 | |
F | SER53 | |
B | SER53 | |
A | SER53 |
site_id | SWS_FT_FI13 |
Number of Residues | 12 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q5SWU9 |
Chain | Residue | Details |
D | THR58 | |
B | THR1227 | |
A | THR58 | |
A | THR1227 | |
D | THR1227 | |
E | THR58 | |
E | THR1227 | |
C | THR58 | |
C | THR1227 | |
F | THR58 | |
F | THR1227 | |
B | THR58 |
site_id | SWS_FT_FI14 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:29899443, ECO:0000269|Ref.9, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
D | SER80 | |
E | SER80 | |
C | SER80 | |
F | SER80 | |
B | SER80 | |
A | SER80 |
site_id | SWS_FT_FI15 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336 |
Chain | Residue | Details |
D | SER488 | |
E | SER488 | |
C | SER488 | |
F | SER488 | |
B | SER488 | |
A | SER488 |
site_id | SWS_FT_FI16 |
Number of Residues | 12 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
D | THR610 | |
B | THR2153 | |
A | THR610 | |
A | THR2153 | |
D | THR2153 | |
E | THR610 | |
E | THR2153 | |
C | THR610 | |
C | THR2153 | |
F | THR610 | |
F | THR2153 | |
B | THR610 |
site_id | SWS_FT_FI17 |
Number of Residues | 6 |
Details | MOD_RES: N6-biotinyllysine => ECO:0000250|UniProtKB:P11497, ECO:0000255|PROSITE-ProRule:PRU01066 |
Chain | Residue | Details |
D | LYS786 | |
E | LYS786 | |
C | LYS786 | |
F | LYS786 | |
B | LYS786 | |
A | LYS786 |
site_id | SWS_FT_FI18 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
D | SER835 | |
E | SER835 | |
C | SER835 | |
F | SER835 | |
B | SER835 | |
A | SER835 |
site_id | SWS_FT_FI19 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5SWU9 |
Chain | Residue | Details |
D | SER1218 | |
B | SER1259 | |
A | SER1218 | |
A | SER1259 | |
D | SER1259 | |
E | SER1218 | |
E | SER1259 | |
C | SER1218 | |
C | SER1259 | |
F | SER1218 | |
F | SER1259 | |
B | SER1218 |
site_id | SWS_FT_FI20 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16698035, ECO:0000269|PubMed:29899443 |
Chain | Residue | Details |
D | SER1263 | |
E | SER1263 | |
C | SER1263 | |
F | SER1263 | |
B | SER1263 | |
A | SER1263 |
site_id | SWS_FT_FI21 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
D | SER1273 | |
E | SER1273 | |
C | SER1273 | |
F | SER1273 | |
B | SER1273 | |
A | SER1273 |
site_id | SWS_FT_FI22 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
D | LYS1334 | |
E | LYS1334 | |
C | LYS1334 | |
F | LYS1334 | |
B | LYS1334 | |
A | LYS1334 |