2gci
The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an asparte/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
1. Protein Identity and Related Structures Protein Identity & Related Structures
No usable UniProt protein identity is available for this entry.
The relationship tables retain this entry's assembly and composition data, but cross-PDB links for the same protein cannot be established reliably without a unified protein identity.
Assembly Composition of the Current Entry
| Assembly | Physical composition | Protein state | 蛋白 / DNA / RNA / 其他Polymer | Data consistency |
|---|---|---|---|---|
| 1 | Protein homooligomer | Homooligomer | 2 / 0 / 0 / 0 | Consistent with protein count |
| 2 | Protein homooligomer | Homooligomer | 2 / 0 / 0 / 0 | Consistent with protein count |
The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.
2. Structure Basics 2. Structure Basics
| Entry ID entry_id | 2gci |
| Deposition date deposition_date | 2006-03-14 |
| Structure title title | The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an asparte/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety |
| Keywords keywords | Alpha-methylacyl-CoA racemase, racemase, CoA transferase, proton transfer, Coenzyme A, ISOMERASE; ISOMERASE |
| Experimental Method method | X-RAY DIFFRACTION |
3. Official assembly/model SAXS Official SAXS Profiles
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
2gci__assembly_1__model_1
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
2gci__assembly_1__model_1 | I(q)
2gci__assembly_1__model_1 | P(r) · Pending
| Rg（Guinier） | 25.91 Å |
| Rg (electron density) | 24.73 Å |
| Total Rg | 25.51 Å |
| Atom count | 5495 |
| Residues | 708 |
| Excluded volume | 96957 ų |
| Maximum q | 0.500 Å⁻¹ |
4. Crystallography and Experiment 4. Crystallography & Experiment
5. Entities and Polymers Entities & Polymers (4)
6. Fold Classification (SCOP + CATH) 12 domains
SCOP 2.08 (4 domains)
| Domain ID domain_id | d2gcia_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.123 — CoA-transferase family III (CaiB/BaiF) |
| Superfamily Superfamily superfamily | c.123.1 — CoA-transferase family III (CaiB/BaiF) |
| Family Family family | c.123.1.1 — CoA-transferase family III (CaiB/BaiF) |
| Domain ID domain_id | d2gcib_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.123 — CoA-transferase family III (CaiB/BaiF) |
| Superfamily Superfamily superfamily | c.123.1 — CoA-transferase family III (CaiB/BaiF) |
| Family Family family | c.123.1.1 — CoA-transferase family III (CaiB/BaiF) |
| Domain ID domain_id | d2gcic_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.123 — CoA-transferase family III (CaiB/BaiF) |
| Superfamily Superfamily superfamily | c.123.1 — CoA-transferase family III (CaiB/BaiF) |
| Family Family family | c.123.1.1 — CoA-transferase family III (CaiB/BaiF) |
| Domain ID domain_id | d2gcid_ |
| Class class | c — Alpha and beta proteins (a/b) |
| Fold Fold fold | c.123 — CoA-transferase family III (CaiB/BaiF) |
| Superfamily Superfamily superfamily | c.123.1 — CoA-transferase family III (CaiB/BaiF) |
| Family Family family | c.123.1.1 — CoA-transferase family III (CaiB/BaiF) |
CATH v4.4 (8 domains)
| Domain ID domain_id | 2gciA01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 50 — Rossmann fold |
| Homologous superfamily homologous superfamily | 10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1 |
| Domain ID domain_id | 2gciA02 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 1540 — formyl-coa transferase, domain 3 |
| Homologous superfamily homologous superfamily | 10 — formyl-coa transferase, domain 3 |
| Domain ID domain_id | 2gciB01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 50 — Rossmann fold |
| Homologous superfamily homologous superfamily | 10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1 |
| Domain ID domain_id | 2gciB02 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 1540 — formyl-coa transferase, domain 3 |
| Homologous superfamily homologous superfamily | 10 — formyl-coa transferase, domain 3 |
| Domain ID domain_id | 2gciC01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 50 — Rossmann fold |
| Homologous superfamily homologous superfamily | 10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1 |
| Domain ID domain_id | 2gciC02 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 1540 — formyl-coa transferase, domain 3 |
| Homologous superfamily homologous superfamily | 10 — formyl-coa transferase, domain 3 |
| Domain ID domain_id | 2gciD01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| Topology topology | 50 — Rossmann fold |
| Homologous superfamily homologous superfamily | 10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1 |
| Domain ID domain_id | 2gciD02 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 30 — 2-Layer Sandwich |
| Topology topology | 1540 — formyl-coa transferase, domain 3 |
| Homologous superfamily homologous superfamily | 10 — formyl-coa transferase, domain 3 |