3UKL
Crystal structure of UDP-galactopyranose mutase from Aspergillus fumigatus in complex with UDP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0071555 | biological_process | cell wall organization |
B | 0000166 | molecular_function | nucleotide binding |
B | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0071555 | biological_process | cell wall organization |
C | 0000166 | molecular_function | nucleotide binding |
C | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0071555 | biological_process | cell wall organization |
D | 0000166 | molecular_function | nucleotide binding |
D | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0071555 | biological_process | cell wall organization |
E | 0000166 | molecular_function | nucleotide binding |
E | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
E | 0016853 | molecular_function | isomerase activity |
E | 0071555 | biological_process | cell wall organization |
F | 0000166 | molecular_function | nucleotide binding |
F | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
F | 0016853 | molecular_function | isomerase activity |
F | 0071555 | biological_process | cell wall organization |
G | 0000166 | molecular_function | nucleotide binding |
G | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
G | 0016853 | molecular_function | isomerase activity |
G | 0071555 | biological_process | cell wall organization |
H | 0000166 | molecular_function | nucleotide binding |
H | 0008767 | molecular_function | UDP-galactopyranose mutase activity |
H | 0016853 | molecular_function | isomerase activity |
H | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE UDP A 800 |
Chain | Residue |
A | TYR104 |
A | VAL183 |
A | TYR317 |
A | ARG327 |
A | TYR419 |
A | TYR453 |
A | HOH554 |
A | HOH1052 |
A | PHE106 |
A | GLN107 |
A | PHE142 |
A | PHE158 |
A | MET159 |
A | ASN163 |
A | TRP167 |
A | ARG182 |
site_id | AC2 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD A 602 |
Chain | Residue |
A | GLY14 |
A | GLY16 |
A | PRO17 |
A | THR18 |
A | ASP38 |
A | SER39 |
A | GLY45 |
A | LEU46 |
A | VAL60 |
A | GLY62 |
A | HIS63 |
A | VAL64 |
A | GLY240 |
A | LYS241 |
A | VAL242 |
A | MET269 |
A | THR295 |
A | GLU373 |
A | GLY418 |
A | TYR419 |
A | GLY446 |
A | ARG447 |
A | GLY456 |
A | ASN457 |
A | GLN458 |
A | SER461 |
A | HOH653 |
A | HOH798 |
A | HOH807 |
A | HOH833 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1 |
Chain | Residue |
A | GLN358 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 512 |
Chain | Residue |
A | ALA270 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE UDP B 800 |
Chain | Residue |
B | VAL95 |
B | TYR104 |
B | PHE106 |
B | GLN107 |
B | PHE158 |
B | MET159 |
B | ASN163 |
B | TRP167 |
B | ARG182 |
B | VAL183 |
B | TYR317 |
B | ARG327 |
B | TYR419 |
B | TYR453 |
B | HOH566 |
B | HOH936 |
B | HOH1053 |
site_id | AC6 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD B 604 |
Chain | Residue |
B | GLY14 |
B | GLY16 |
B | PRO17 |
B | THR18 |
B | ASP38 |
B | SER39 |
B | GLY45 |
B | LEU46 |
B | VAL60 |
B | GLY62 |
B | HIS63 |
B | VAL64 |
B | GLY240 |
B | VAL242 |
B | THR295 |
B | GLU373 |
B | GLY418 |
B | TYR419 |
B | GLY446 |
B | ARG447 |
B | GLY456 |
B | ASN457 |
B | GLN458 |
B | SER461 |
B | HOH558 |
B | HOH588 |
B | HOH605 |
B | HOH606 |
B | HOH808 |
site_id | AC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE UDP C 800 |
Chain | Residue |
C | MET159 |
C | ASN163 |
C | TRP167 |
C | ARG182 |
C | VAL183 |
C | TYR317 |
C | ARG327 |
C | TYR419 |
C | TYR453 |
C | HOH589 |
C | HOH969 |
C | HOH1054 |
C | VAL95 |
C | TYR104 |
C | PHE106 |
C | GLN107 |
C | PHE158 |
site_id | AC8 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE FAD C 600 |
Chain | Residue |
C | GLY14 |
C | GLY16 |
C | PRO17 |
C | THR18 |
C | ASP38 |
C | SER39 |
C | GLY45 |
C | LEU46 |
C | VAL60 |
C | HIS63 |
C | VAL64 |
C | GLY240 |
C | VAL242 |
C | MET269 |
C | GLU373 |
C | GLY418 |
C | GLY446 |
C | ARG447 |
C | GLY456 |
C | ASN457 |
C | GLN458 |
C | SER461 |
C | HOH514 |
C | HOH519 |
C | HOH619 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL C 1 |
Chain | Residue |
C | GLN358 |
C | HOH618 |
site_id | BC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE UDP D 800 |
Chain | Residue |
D | VAL95 |
D | TYR104 |
D | PHE106 |
D | GLN107 |
D | PHE142 |
D | PHE158 |
D | MET159 |
D | ASN163 |
D | TRP167 |
D | ARG182 |
D | VAL183 |
D | TYR317 |
D | ARG327 |
D | TYR419 |
D | TYR453 |
D | HOH546 |
site_id | BC2 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD D 601 |
Chain | Residue |
D | GLY14 |
D | GLY16 |
D | PRO17 |
D | THR18 |
D | ASP38 |
D | SER39 |
D | GLY45 |
D | LEU46 |
D | ALA47 |
D | VAL60 |
D | GLY62 |
D | HIS63 |
D | VAL64 |
D | GLY240 |
D | LYS241 |
D | VAL242 |
D | MET269 |
D | THR295 |
D | GLU373 |
D | GLY418 |
D | TYR419 |
D | GLY446 |
D | ARG447 |
D | GLY456 |
D | ASN457 |
D | GLN458 |
D | SER461 |
D | HOH517 |
D | HOH558 |
D | HOH585 |
D | HOH799 |
site_id | BC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UDP E 800 |
Chain | Residue |
E | TYR104 |
E | PHE106 |
E | GLN107 |
E | PHE158 |
E | MET159 |
E | ASN163 |
E | TRP167 |
E | ARG182 |
E | VAL183 |
E | TYR317 |
E | ARG327 |
E | TYR419 |
E | TYR453 |
E | HOH547 |
E | HOH576 |
site_id | BC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD E 606 |
Chain | Residue |
E | GLY14 |
E | GLY16 |
E | PRO17 |
E | THR18 |
E | ASP38 |
E | SER39 |
E | GLY45 |
E | LEU46 |
E | VAL60 |
E | GLY62 |
E | HIS63 |
E | VAL64 |
E | GLY240 |
E | VAL242 |
E | MET269 |
E | THR295 |
E | GLU373 |
E | GLY418 |
E | TYR419 |
E | GLY446 |
E | ARG447 |
E | GLY456 |
E | ASN457 |
E | GLN458 |
E | SER461 |
E | HOH517 |
E | HOH558 |
E | HOH586 |
E | HOH809 |
site_id | BC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE UDP F 800 |
Chain | Residue |
F | VAL95 |
F | TYR104 |
F | PHE106 |
F | GLN107 |
F | PHE158 |
F | MET159 |
F | ASN163 |
F | TRP167 |
F | ARG182 |
F | VAL183 |
F | TYR317 |
F | ARG327 |
F | TYR419 |
F | TYR453 |
F | HOH555 |
F | HOH564 |
site_id | BC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD F 603 |
Chain | Residue |
F | GLY14 |
F | GLY16 |
F | PRO17 |
F | THR18 |
F | ASP38 |
F | SER39 |
F | GLY45 |
F | LEU46 |
F | ALA47 |
F | VAL60 |
F | GLY62 |
F | HIS63 |
F | VAL64 |
F | GLY240 |
F | VAL242 |
F | MET269 |
F | THR295 |
F | GLU373 |
F | GLY418 |
F | TYR419 |
F | GLY446 |
F | ARG447 |
F | GLY456 |
F | ASN457 |
F | GLN458 |
F | SER461 |
F | HOH513 |
F | HOH515 |
site_id | BC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL F 1 |
Chain | Residue |
F | GLN358 |
site_id | BC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL F 512 |
Chain | Residue |
F | ALA270 |
site_id | BC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE UDP G 800 |
Chain | Residue |
G | TYR104 |
G | PHE106 |
G | GLN107 |
G | PHE158 |
G | MET159 |
G | ASN163 |
G | TRP167 |
G | ARG182 |
G | VAL183 |
G | TYR317 |
G | ARG327 |
G | TYR419 |
G | TYR453 |
G | HOH1049 |
site_id | CC1 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD G 607 |
Chain | Residue |
G | GLY14 |
G | GLY16 |
G | PRO17 |
G | THR18 |
G | ASP38 |
G | SER39 |
G | GLY45 |
G | LEU46 |
G | ALA47 |
G | VAL60 |
G | HIS63 |
G | VAL64 |
G | GLY240 |
G | LYS241 |
G | VAL242 |
G | MET269 |
G | THR295 |
G | GLU373 |
G | GLY418 |
G | TYR419 |
G | GLY446 |
G | ARG447 |
G | GLY456 |
G | ASN457 |
G | GLN458 |
G | SER461 |
G | HOH512 |
G | HOH554 |
G | HOH556 |
site_id | CC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UDP H 800 |
Chain | Residue |
H | VAL95 |
H | TYR104 |
H | PHE106 |
H | GLN107 |
H | PHE158 |
H | MET159 |
H | ASN163 |
H | TRP167 |
H | ARG182 |
H | VAL183 |
H | TYR317 |
H | ARG327 |
H | TYR419 |
H | TYR453 |
H | HOH875 |
site_id | CC3 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD H 605 |
Chain | Residue |
H | GLY14 |
H | GLY16 |
H | PRO17 |
H | THR18 |
H | ASP38 |
H | SER39 |
H | GLY45 |
H | LEU46 |
H | VAL60 |
H | GLY62 |
H | HIS63 |
H | VAL64 |
H | GLY240 |
H | VAL242 |
H | MET269 |
H | THR295 |
H | GLU373 |
H | GLY418 |
H | TYR419 |
H | GLY446 |
H | ARG447 |
H | GLY456 |
H | ASN457 |
H | GLN458 |
H | SER461 |
H | HOH806 |
H | HOH810 |
site_id | CC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL H 1 |
Chain | Residue |
H | GLN358 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 64 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22294687, ECO:0000269|PubMed:22334662, ECO:0007744|PDB:3UKA, ECO:0007744|PDB:3UKH, ECO:0007744|PDB:3UKK, ECO:0007744|PDB:3UKL, ECO:0007744|PDB:3UKP, ECO:0007744|PDB:3UTE |
Chain | Residue | Details |
A | THR18 | |
B | ASP38 | |
B | LEU46 | |
B | HIS63 | |
B | VAL242 | |
B | GLY456 | |
B | GLN458 | |
B | SER461 | |
C | THR18 | |
C | ASP38 | |
C | LEU46 | |
A | ASP38 | |
C | HIS63 | |
C | VAL242 | |
C | GLY456 | |
C | GLN458 | |
C | SER461 | |
D | THR18 | |
D | ASP38 | |
D | LEU46 | |
D | HIS63 | |
D | VAL242 | |
A | LEU46 | |
D | GLY456 | |
D | GLN458 | |
D | SER461 | |
E | THR18 | |
E | ASP38 | |
E | LEU46 | |
E | HIS63 | |
E | VAL242 | |
E | GLY456 | |
E | GLN458 | |
A | HIS63 | |
E | SER461 | |
F | THR18 | |
F | ASP38 | |
F | LEU46 | |
F | HIS63 | |
F | VAL242 | |
F | GLY456 | |
F | GLN458 | |
F | SER461 | |
G | THR18 | |
A | VAL242 | |
G | ASP38 | |
G | LEU46 | |
G | HIS63 | |
G | VAL242 | |
G | GLY456 | |
G | GLN458 | |
G | SER461 | |
H | THR18 | |
H | ASP38 | |
H | LEU46 | |
A | GLY456 | |
H | HIS63 | |
H | VAL242 | |
H | GLY456 | |
H | GLN458 | |
H | SER461 | |
A | GLN458 | |
A | SER461 | |
B | THR18 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22334662, ECO:0007744|PDB:3UKP |
Chain | Residue | Details |
A | GLY61 | |
B | GLY61 | |
C | GLY61 | |
D | GLY61 | |
E | GLY61 | |
F | GLY61 | |
G | GLY61 | |
H | GLY61 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22334662, ECO:0007744|PDB:3UKF, ECO:0007744|PDB:3UKP, ECO:0007744|PDB:3UKQ |
Chain | Residue | Details |
A | GLY62 | |
B | GLY62 | |
C | GLY62 | |
D | GLY62 | |
E | GLY62 | |
F | GLY62 | |
G | GLY62 | |
H | GLY62 |
site_id | SWS_FT_FI4 |
Number of Residues | 56 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23036087, ECO:0007744|PDB:5VWT |
Chain | Residue | Details |
A | HIS68 | |
B | SER93 | |
B | ASN203 | |
B | TRP315 | |
B | ARG447 | |
B | HIS460 | |
C | HIS68 | |
C | ARG91 | |
C | SER93 | |
C | ASN203 | |
C | TRP315 | |
A | ARG91 | |
C | ARG447 | |
C | HIS460 | |
D | HIS68 | |
D | ARG91 | |
D | SER93 | |
D | ASN203 | |
D | TRP315 | |
D | ARG447 | |
D | HIS460 | |
E | HIS68 | |
A | SER93 | |
E | ARG91 | |
E | SER93 | |
E | ASN203 | |
E | TRP315 | |
E | ARG447 | |
E | HIS460 | |
F | HIS68 | |
F | ARG91 | |
F | SER93 | |
F | ASN203 | |
A | ASN203 | |
F | TRP315 | |
F | ARG447 | |
F | HIS460 | |
G | HIS68 | |
G | ARG91 | |
G | SER93 | |
G | ASN203 | |
G | TRP315 | |
G | ARG447 | |
G | HIS460 | |
A | TRP315 | |
H | HIS68 | |
H | ARG91 | |
H | SER93 | |
H | ASN203 | |
H | TRP315 | |
H | ARG447 | |
H | HIS460 | |
A | ARG447 | |
A | HIS460 | |
B | HIS68 | |
B | ARG91 |
site_id | SWS_FT_FI5 |
Number of Residues | 64 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22294687, ECO:0000269|PubMed:22334662, ECO:0007744|PDB:3UKF, ECO:0007744|PDB:3UKH, ECO:0007744|PDB:3UKP, ECO:0007744|PDB:3UKQ, ECO:0007744|PDB:3UTH |
Chain | Residue | Details |
A | TYR104 | |
B | GLN107 | |
B | ASN163 | |
B | TRP167 | |
B | ARG182 | |
B | ASN207 | |
B | TYR419 | |
B | TYR453 | |
C | TYR104 | |
C | GLN107 | |
C | ASN163 | |
A | GLN107 | |
C | TRP167 | |
C | ARG182 | |
C | ASN207 | |
C | TYR419 | |
C | TYR453 | |
D | TYR104 | |
D | GLN107 | |
D | ASN163 | |
D | TRP167 | |
D | ARG182 | |
A | ASN163 | |
D | ASN207 | |
D | TYR419 | |
D | TYR453 | |
E | TYR104 | |
E | GLN107 | |
E | ASN163 | |
E | TRP167 | |
E | ARG182 | |
E | ASN207 | |
E | TYR419 | |
A | TRP167 | |
E | TYR453 | |
F | TYR104 | |
F | GLN107 | |
F | ASN163 | |
F | TRP167 | |
F | ARG182 | |
F | ASN207 | |
F | TYR419 | |
F | TYR453 | |
G | TYR104 | |
A | ARG182 | |
G | GLN107 | |
G | ASN163 | |
G | TRP167 | |
G | ARG182 | |
G | ASN207 | |
G | TYR419 | |
G | TYR453 | |
H | TYR104 | |
H | GLN107 | |
H | ASN163 | |
A | ASN207 | |
H | TRP167 | |
H | ARG182 | |
H | ASN207 | |
H | TYR419 | |
H | TYR453 | |
A | TYR419 | |
A | TYR453 | |
B | TYR104 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22334662, ECO:0007744|PDB:3UKH, ECO:0007744|PDB:3UKP |
Chain | Residue | Details |
A | MET159 | |
E | TYR162 | |
F | MET159 | |
F | TYR162 | |
G | MET159 | |
G | TYR162 | |
H | MET159 | |
H | TYR162 | |
A | TYR162 | |
B | MET159 | |
B | TYR162 | |
C | MET159 | |
C | TYR162 | |
D | MET159 | |
D | TYR162 | |
E | MET159 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22294687, ECO:0000269|PubMed:22334662, ECO:0007744|PDB:3UKH, ECO:0007744|PDB:3UKQ, ECO:0007744|PDB:3UTH |
Chain | Residue | Details |
A | TYR317 | |
B | TYR317 | |
C | TYR317 | |
D | TYR317 | |
E | TYR317 | |
F | TYR317 | |
G | TYR317 | |
H | TYR317 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22294687, ECO:0000269|PubMed:22334662, ECO:0007744|PDB:3UKF, ECO:0007744|PDB:3UKH, ECO:0007744|PDB:3UTH |
Chain | Residue | Details |
A | ARG327 | |
B | ARG327 | |
C | ARG327 | |
D | ARG327 | |
E | ARG327 | |
F | ARG327 | |
G | ARG327 | |
H | ARG327 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22334662, ECO:0007744|PDB:3UKH |
Chain | Residue | Details |
A | ASN457 | |
B | ASN457 | |
C | ASN457 | |
D | ASN457 | |
E | ASN457 | |
F | ASN457 | |
G | ASN457 | |
H | ASN457 |