5IKP
Crystal structure of human brain glycogen phosphorylase bound to AMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005977 | biological_process | glycogen metabolic process |
| A | 0005980 | biological_process | glycogen catabolic process |
| A | 0008184 | molecular_function | glycogen phosphorylase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0035578 | cellular_component | azurophil granule lumen |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
| A | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue PLP A 901 |
| Chain | Residue |
| A | TYR90 |
| A | LYS680 |
| A | LYS568 |
| A | ARG569 |
| A | LYS574 |
| A | ARG649 |
| A | ALA653 |
| A | GLY675 |
| A | THR676 |
| A | GLY677 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue AMP A 902 |
| Chain | Residue |
| A | ASP42 |
| A | ASN44 |
| A | VAL45 |
| A | GLN71 |
| A | GLN72 |
| A | TYR75 |
| A | TYR196 |
| A | ARG309 |
| A | ARG310 |
Functional Information from PROSITE/UniProt
| site_id | PS00102 |
| Number of Residues | 13 |
| Details | PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN |
| Chain | Residue | Details |
| A | GLU672-ASN684 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27402852 |
| Chain | Residue | Details |
| A | LYS568 | |
| A | ASP42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:27402852 |
| Chain | Residue | Details |
| A | TYR196 | |
| A | ARG309 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Participates in a stacking interaction with the adenine ring of AMP => ECO:0000269|PubMed:27402852 |
| Chain | Residue | Details |
| A | TYR75 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Involved in the association of subunits => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS142 | |
| A | CYS108 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: May be involved in allosteric control => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR155 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | ALA1 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P53534 |
| Chain | Residue | Details |
| A | SER14 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q8CI94 |
| Chain | Residue | Details |
| A | TYR472 | |
| A | TYR196 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:27402852 |
| Chain | Residue | Details |
| A | LYS680 |
